{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397SYF5","uniProtkbId":"A0A397SYF5_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":28,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA91003.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Pentafunctional AROM polypeptide"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"DHQS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"4.2.3.4"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-phosphoshikimate 1-carboxyvinyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"2.5.1.19"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"5-enolpyruvylshikimate-3-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"EPSP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"EPSPS"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Shikimate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"SK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"2.7.1.71"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinate dehydratase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"4.2.1.10"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Shikimate dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"1.1.1.25"}]}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA91003.1"}],"value":"C1645_822575"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-dehydroquinate = 3-dehydroshikimate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21096"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:32364"}],"ecNumber":"4.2.1.10","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21256"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57701"},{"database":"ChEBI","id":"CHEBI:58702"},{"database":"ChEBI","id":"CHEBI:145989"}],"ecNumber":"2.5.1.19","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044633"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21257"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044633"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21968"},{"database":"ChEBI","id":"CHEBI:32364"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58394"}],"ecNumber":"4.2.3.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + ATP = 3-phosphoshikimate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13121"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:145989"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048567"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + NADP(+) = 3-dehydroshikimate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17737"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.1.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004811"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009948"}],"value":"Belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 2nd section; belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 3rd section; belongs to the shikimate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 4th section; belongs to the type-I 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the C-terminal section; belongs to the shikimate dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the N-terminal section; belongs to the dehydroquinate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA91003.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01761"}]},{"type":"Domain","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF24621"}]},{"type":"Domain","location":{"start":{"value":426,"modifier":"EXACT"},"end":{"value":863,"modifier":"EXACT"}},"description":"Enolpyruvate transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00275"}]},{"type":"Domain","location":{"start":{"value":1288,"modifier":"EXACT"},"end":{"value":1368,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase substrate binding N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08501"}]},{"type":"Domain","location":{"start":{"value":1519,"modifier":"EXACT"},"end":{"value":1548,"modifier":"EXACT"}},"description":"SDH C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF18317"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Region","location":{"start":{"value":1283,"modifier":"EXACT"},"end":{"value":1554,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":851,"modifier":"EXACT"},"end":{"value":851,"modifier":"EXACT"}},"description":"For EPSP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":1173,"modifier":"EXACT"},"end":{"value":1173,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":1201,"modifier":"EXACT"},"end":{"value":1201,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Binding site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":887,"modifier":"EXACT"},"end":{"value":894,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA91003.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA91003.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000164","properties":[{"key":"ProteinId","value":"RIA91003.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"STRING","id":"658196.A0A397SYF5","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"197068at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00053","properties":[{"key":"RectionId","value":"UER00085"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003855","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003856","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003866","properties":[{"key":"GoTerm","value":"F:3-phosphoshikimate 1-carboxyvinyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004764","properties":[{"key":"GoTerm","value":"F:shikimate 3-dehydrogenase (NADP+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004765","properties":[{"key":"GoTerm","value":"F:shikimate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009073","properties":[{"key":"GoTerm","value":"P:aromatic amino acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009423","properties":[{"key":"GoTerm","value":"P:chorismate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00502","properties":[{"key":"EntryName","value":"DHQase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08195","properties":[{"key":"EntryName","value":"DHQS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01556","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01065","properties":[{"key":"EntryName","value":"NAD_bind_Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00464","properties":[{"key":"EntryName","value":"SK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1090.10:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000135","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1970:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.65.10.10:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.65.10.10:FF:000008","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1090.10","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like - alpha domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.65.10.10","properties":[{"key":"EntryName","value":"Enolpyruvate transferase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.10860","properties":[{"key":"EntryName","value":"Leucine Dehydrogenase, chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00210","properties":[{"key":"EntryName","value":"EPSP_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03143","properties":[{"key":"EntryName","value":"Pentafunct_AroM"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00109","properties":[{"key":"EntryName","value":"Shikimate_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR046346","properties":[{"key":"EntryName","value":"Aminoacid_DH-like_N_sf"}]},{"database":"InterPro","id":"IPR016037","properties":[{"key":"EntryName","value":"DHQ_synth_AroB"}]},{"database":"InterPro","id":"IPR030960","properties":[{"key":"EntryName","value":"DHQS/DOIS_N"}]},{"database":"InterPro","id":"IPR056179","properties":[{"key":"EntryName","value":"DHQS_C"}]},{"database":"InterPro","id":"IPR001381","properties":[{"key":"EntryName","value":"DHquinase_I"}]},{"database":"InterPro","id":"IPR001986","properties":[{"key":"EntryName","value":"Enolpyruvate_Tfrase_dom"}]},{"database":"InterPro","id":"IPR036968","properties":[{"key":"EntryName","value":"Enolpyruvate_Tfrase_sf"}]},{"database":"InterPro","id":"IPR006264","properties":[{"key":"EntryName","value":"EPSP_synthase"}]},{"database":"InterPro","id":"IPR023193","properties":[{"key":"EntryName","value":"EPSP_synthase_CS"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR008289","properties":[{"key":"EntryName","value":"Pentafunct_AroM"}]},{"database":"InterPro","id":"IPR013792","properties":[{"key":"EntryName","value":"RNA3'P_cycl/enolpyr_Trfase_a/b"}]},{"database":"InterPro","id":"IPR041121","properties":[{"key":"EntryName","value":"SDH_C"}]},{"database":"InterPro","id":"IPR031322","properties":[{"key":"EntryName","value":"Shikimate/glucono_kinase"}]},{"database":"InterPro","id":"IPR013708","properties":[{"key":"EntryName","value":"Shikimate_DH-bd_N"}]},{"database":"InterPro","id":"IPR010110","properties":[{"key":"EntryName","value":"Shikimate_DH_AroM-type"}]},{"database":"InterPro","id":"IPR000623","properties":[{"key":"EntryName","value":"Shikimate_kinase/TSH1"}]},{"database":"InterPro","id":"IPR023000","properties":[{"key":"EntryName","value":"Shikimate_kinase_CS"}]},{"database":"NCBIfam","id":"TIGR01356","properties":[{"key":"EntryName","value":"aroA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01357","properties":[{"key":"EntryName","value":"aroB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01093","properties":[{"key":"EntryName","value":"aroD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01809","properties":[{"key":"EntryName","value":"Shik-DH-AROM"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21090","properties":[{"key":"EntryName","value":"AROM/DEHYDROQUINATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21090:SF5","properties":[{"key":"EntryName","value":"PENTAFUNCTIONAL AROM POLYPEPTIDE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01761","properties":[{"key":"EntryName","value":"DHQ_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF24621","properties":[{"key":"EntryName","value":"DHQS_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01487","properties":[{"key":"EntryName","value":"DHquinase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00275","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18317","properties":[{"key":"EntryName","value":"SDH_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08501","properties":[{"key":"EntryName","value":"Shikimate_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01202","properties":[{"key":"EntryName","value":"SKI"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000514","properties":[{"key":"EntryName","value":"Pentafunct_AroM"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01100","properties":[{"key":"EntryName","value":"SHIKIMTKNASE"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53223","properties":[{"key":"EntryName","value":"Aminoacid dehydrogenase-like, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56796","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55205","properties":[{"key":"EntryName","value":"EPT/RTPC-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00104","properties":[{"key":"EntryName","value":"EPSP_SYNTHASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00885","properties":[{"key":"EntryName","value":"EPSP_SYNTHASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01128","properties":[{"key":"EntryName","value":"SHIKIMATE_KINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTLLEQPEPDIIKVSILNEESIILGFHLTKFMIRDVISNIPSSTYVIITDKNIAPIYLTKIVEDFNIIASEITLAKGKNALKPRLITYIIPPGEQTKSRDTKAEIEDFLLSKACARDTCILAMGGGVIGDLVGFVAATFMRGVPFVQIPTTLLAMVDSSIGGKTAIDTPHGKNLIGSFWQPKRIYIDLIFLETLPEREFINGMAEVIKTAAISSESDFIILENGVEKIREAVLNPKRDVPFQGAKLETRTPSQSLLLSVIMASAQFKAYVVTHDEREGGLRGLLNFGHTIGHAIEAIMYPELLHGECVSIGMIKEAEIARHLGYLNQVAISRLYKILQDYGLPVSLEEKKVKDLVGKKFCAVDKLMEIMKVDKKIQGDQKRIVILSSIGNTYEKKATVVSDSVIHKILSPAIKVLPVTSSPNISSIHITMTTPGSKSISNRALILAALGVGTCKLKSLLYSDDTQVMMVALQNLGAAKFEWENNGEVLIVTGGGGNLQIPDNELYLGNAGTASRFLTTVCTLISAETATQTKMHTILTGNARMKQRPIGPLVTTLQENGSQIRYVENEGSLPIEITPSQTKFKGGKINLAASISSQYVSSILLSAPYASEPVTLSLTGGKVVSQPYIDMTIAMMKSFGIEVKRLEDNVYYIPQGKYTNPSEYVIESDASSATYPLAVAAITGITCTLPNIGASSLQGDAAFAVKVLKPMGCTVTQTETSTTVKGPPIGSLRPLPNIDMETMTDAFLTASVLAAVASNSDEGEECITRITGISNQRVKECNRIAAMVHELTKFGVVASELPDGIQIHGSKTQSLKGPASGVKCYDDHRIAMSFSILGCVIPDGTIILEKKCVEKTWPGWWDDLESKLGINLLGVDIGSDQESIIFIGMRGAGKTTLGKDVAKALNREFLDLDHHFESLLSTTISKFIEEEGWDAFRAKEFEILKSVLSTHSSGHIIACGGGIVEHPSSRDLLKQYSQNHGDVVHIVRDINDVIRYLNKDNSRPSFDDELLNVWNKREIWYNECSNLDNKIGGSSIDNLIEIIRKTKRTFFVSLTLPDITPALKDLPTITHGVDAIEFRVDLLSENGNLPSVEYIFNQLEILRRASSLPIIFTVRSQSQGGKYPDTQEKEMFLLLEQAIKSGCEYIDVEILMSPSLISNLIEKKGNAKIIASWHDISGITKWDGEEVRQRFRAAQNIGDIIKIVGRASCLSDNFKLRNFVELQQQHCKKPIIAINMETEGQLSRILNQYFTPVTHPLLPSKAASGQLSVAEIHKGLHLIGQLPKKKFYLFGTPIAHSMSPTIHNTGFDVLGLPYHYDLFESEDVKAVKPIIEDIEFGGASVTIPHKINIIPLLDQITEQSKLIGAVNTITVMESEAGRKLIGDNTDWLGIFYSIKPLIEIDSKTTGLVIGGGGTSRAGIFALHQLGVSTIYLYNRTQDKIKELIDQFPTYGIIGLSSLSEPIQNPPRIIVSTIPATSNLEIPNEIFSSGKGGVIVEMAYKPRRTQLLKKGDEKEWIGVEGVQVLIEQGLCQFEKWTGRKAPRNIIEEIVYKKYDS","length":1554,"molWeight":170634,"crc64":"365CDD499CDFF3C6","md5":"BB0C46A331581AD7A2E24D3CACFD63FC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"COFACTOR":1,"PATHWAY":5,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":7,"CAUTION":2},"countByFeatureType":{"Domain":5,"Region":2,"Active site":5,"Binding site":20},"uniParcId":"UPI000EE900D5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397T7I2","uniProtkbId":"A0A397T7I2_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":28,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92197.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024439"}],"value":"ATP-binding cassette sub-family B member 6"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024385"}],"value":"7.6.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031413"}],"value":"ABC-type heme transporter ABCB6"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92197.1"}],"value":"C1645_710937"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"coproporphyrin I(in) + ATP + H2O = coproporphyrin I(out) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66768"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:167478"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049398"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66769"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049398"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"coproporphyrin III(in) + ATP + H2O = coproporphyrin III(out) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66664"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:131725"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048636"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66665"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048636"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"coproporphyrinogen III(in) + ATP + H2O = coproporphyrinogen III(out) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66680"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57309"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047753"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66681"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047753"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"heme b(in) + ATP + H2O = heme b(out) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19261"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"7.6.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047649"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:19262"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047649"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"pheophorbide a(in) + ATP + H2O = pheophorbide a(out) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:61360"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58687"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048455"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:61361"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048455"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"protoporphyrin IX(in) + ATP + H2O = protoporphyrin IX(out) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:61336"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57306"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048309"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:61337"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048309"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uroporphyrin I(in) + ATP + H2O = uroporphyrin I(out) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66772"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:167480"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047789"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66773"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047789"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uroporphyrin III(in) + ATP + H2O = uroporphyrin III(out) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66776"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:167479"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048510"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66777"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048510"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004146"}],"value":"Early endosome membrane","id":"SL-0093"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004477"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004477"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004337"}],"value":"Endosome membrane","id":"SL-0100"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004337"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004333"}],"value":"Endosome, multivesicular body membrane","id":"SL-0175"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004653"}],"value":"Golgi apparatus membrane","id":"SL-0134"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004653"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004414"}],"value":"Late endosome membrane","id":"SL-0151"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004374"}],"value":"Mitochondrion outer membrane","id":"SL-0172"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004374"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004550"}],"value":"Secreted, extracellular exosome","id":"SL-0466"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024363"}],"value":"Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92197.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":413,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":505,"modifier":"EXACT"},"end":{"value":523,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":529,"modifier":"EXACT"},"end":{"value":549,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":558,"modifier":"EXACT"}},"description":"ABC transmembrane type-1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50929"}]},{"type":"Domain","location":{"start":{"value":592,"modifier":"EXACT"},"end":{"value":826,"modifier":"EXACT"}},"description":"ABC transporter","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50893"}]},{"type":"Region","location":{"start":{"value":837,"modifier":"EXACT"},"end":{"value":872,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":625,"modifier":"EXACT"},"end":{"value":632,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00434"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00434"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022824"}],"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022753"}],"id":"KW-0967","category":"Cellular component","name":"Endosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023034"}],"id":"KW-0333","category":"Cellular component","name":"Golgi apparatus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023228"}],"id":"KW-0458","category":"Cellular component","name":"Lysosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022787"}],"id":"KW-1000","category":"Cellular component","name":"Mitochondrion outer membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00434"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022525"}],"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92197.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92197.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000132","properties":[{"key":"ProteinId","value":"RIA92197.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397T7I2","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397T7I2","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"6500128at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0031901","properties":[{"key":"GoTerm","value":"C:early endosome membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005789","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000139","properties":[{"key":"GoTerm","value":"C:Golgi membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005741","properties":[{"key":"GoTerm","value":"C:mitochondrial outer membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0032585","properties":[{"key":"GoTerm","value":"C:multivesicular body membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005774","properties":[{"key":"GoTerm","value":"C:vacuolar membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0015439","properties":[{"key":"GoTerm","value":"F:ABC-type heme transporter activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd18581","properties":[{"key":"EntryName","value":"ABC_6TM_ABCB6"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03253","properties":[{"key":"EntryName","value":"ABCC_ATM1_transporter"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000186","properties":[{"key":"EntryName","value":"ATP-binding cassette sub-family B member 7, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1560.10","properties":[{"key":"EntryName","value":"ABC transporter type 1, transmembrane domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR011527","properties":[{"key":"EntryName","value":"ABC1_TM_dom"}]},{"database":"InterPro","id":"IPR036640","properties":[{"key":"EntryName","value":"ABC1_TM_sf"}]},{"database":"InterPro","id":"IPR003439","properties":[{"key":"EntryName","value":"ABC_transporter-like_ATP-bd"}]},{"database":"InterPro","id":"IPR017871","properties":[{"key":"EntryName","value":"ABC_transporter-like_CS"}]},{"database":"InterPro","id":"IPR032410","properties":[{"key":"EntryName","value":"ABCB6_N"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR039421","properties":[{"key":"EntryName","value":"Type_1_exporter"}]},{"database":"PANTHER","id":"PTHR24221","properties":[{"key":"EntryName","value":"ATP-BINDING CASSETTE SUB-FAMILY B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24221:SF654","properties":[{"key":"EntryName","value":"ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 6"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00664","properties":[{"key":"EntryName","value":"ABC_membrane"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00005","properties":[{"key":"EntryName","value":"ABC_tran"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16185","properties":[{"key":"EntryName","value":"MTABC_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF90123","properties":[{"key":"EntryName","value":"ABC transporter transmembrane region"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50929","properties":[{"key":"EntryName","value":"ABC_TM1F"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00211","properties":[{"key":"EntryName","value":"ABC_TRANSPORTER_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50893","properties":[{"key":"EntryName","value":"ABC_TRANSPORTER_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MENLRVSFTAESPGKTLLFPLSETTLFSVPLFLFVPISLLSYIILFGTYRLVKLRTIEYNPLIDRRRLSPLSRIIYGISGFILLSYLADCAVIIIRALASKVWTSNDIVFYDVGSWAAWVLNLSLMVYERKKLGKWSSVNYCFYFLSLFTDSLVFYYWINQLRSNKPGVIISFYDQALLYIISTRFIFLIIVTFASLIHAFRSSENSESDRGLLGDNSSYGTFPSNNENDQTSQQPSQTEKGAFSDFFEKMGRILPFLWPKKNLMLQILVFVCVGLLVIGRVINVLTPRQLKIITNELIGEDGPPRFAWESIAIYVFLRFLQGGVGLIQSTQNFLWIPIGQYTTREISVKMFEHLHGLSLAYHINRKTGEVLRVMDRGTNSIISLLNQIIFQIFPVLVDIVIAVIYFVFEFGWIFGVIVFFTMGSYIFFTIVITEWRTKFRRDMIELDNDARSKAVDSLLNFETVKYYNAEQYEVKRYDEAIRKFQIADFKVSASLNMLNLSQNLVITIGLLAGCLLCAWKVTLGEFGVGDFILFVTYINQLYGPLNWFGTYYRMIQQNFIDMEKMLLLFKEQQSVKDLPDATELKVTDGSVIFENVGFSYDPRHPALNGISFEIPKGKTVALVGPSGGGKSTILRLLFRFYDADTGRILIDGQDIRTVEQESLRKNIGVVPQDTVLFNDTIYYNIHYGNINASEVEVHKAAKAAQIHDRILNFPDGYETRVGERGLRLSGGEKQRVAIARTILKQPPIILLDEATSALDTTTERQIQYALAQMTQDRTTLVIAHRLSTIVNADLILCIKDGKVVEQGTHDELIRKAEENGGDGIYYEMWQKQIKDESEGKVIVENEGSSKGNDSKNNETSNKGYHGGHPPH","length":872,"molWeight":99239,"crc64":"EC4407D930D33C78","md5":"94D0CFC361F6BD024DCB2F0941431EE5"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":8,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":11,"Domain":2,"Region":1,"Binding site":1},"uniParcId":"UPI000EC51D26"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397TIK0","uniProtkbId":"A0A397TIK0_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":30,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA94831.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00081752"}],"value":"Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013008"}],"value":"2.1.3.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012918"}],"value":"3.5.1.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044063"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012738"}],"value":"6.3.5.5"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA94831.1"}],"value":"C1645_817538"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058513"}],"value":"Multifunctional protein that encodes the first 2 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5) and aspartate transcarbamylase (ATCase; EC 2.1.3.2). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049534"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20013"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:32814"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"}],"ecNumber":"2.1.3.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048859"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004852"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043998"}],"value":"In the 2nd section; belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043968"}],"value":"In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043979"}],"value":"In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043984"}],"value":"In the N-terminal section; belongs to the CarA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA94831.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":617,"modifier":"EXACT"},"end":{"value":809,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1152,"modifier":"EXACT"},"end":{"value":1343,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1409,"modifier":"EXACT"},"end":{"value":1558,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":441,"modifier":"EXACT"},"end":{"value":441,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":443,"modifier":"EXACT"},"end":{"value":443,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA94831.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA94831.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA94831.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000073","properties":[{"key":"ProteinId","value":"RIA94831.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"STRING","id":"658196.A0A397TIK0","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"1924069at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00115"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016597","properties":[{"key":"GoTerm","value":"F:amino acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004070","properties":[{"key":"GoTerm","value":"F:aspartate carbamoyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004151","properties":[{"key":"GoTerm","value":"F:dihydroorotase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006207","properties":[{"key":"GoTerm","value":"P:'de novo' pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0019240","properties":[{"key":"GoTerm","value":"P:L-citrulline biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006228","properties":[{"key":"GoTerm","value":"P:UTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01744","properties":[{"key":"EntryName","value":"GATase1_CPSase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01423","properties":[{"key":"EntryName","value":"MGS_CPS_I_III"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000002","properties":[{"key":"EntryName","value":"Aspartate carbamoyltransferase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000025","properties":[{"key":"EntryName","value":"Bifunctional pyrimidine biosynthesis protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000005","properties":[{"key":"EntryName","value":"CAD protein-like isoform X1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000011","properties":[{"key":"EntryName","value":"CAD protein-like isoform X1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000004","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase (glutamine-hydrolyzing)"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.30.20:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase 1, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.140:FF:000036","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1380:FF:000009","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase, large subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1370","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.50.30.20","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.140","properties":[{"key":"EntryName","value":"Metal-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00001","properties":[{"key":"EntryName","value":"Asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01209","properties":[{"key":"EntryName","value":"CPSase_S_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006132","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoyltranf_P-bd"}]},{"database":"InterPro","id":"IPR006130","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase"}]},{"database":"InterPro","id":"IPR036901","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase_sf"}]},{"database":"InterPro","id":"IPR002082","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf"}]},{"database":"InterPro","id":"IPR006131","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf_Asp/Orn-bd"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR006274","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu"}]},{"database":"InterPro","id":"IPR002474","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu_N"}]},{"database":"InterPro","id":"IPR036480","properties":[{"key":"EntryName","value":"CarbP_synth_ssu_N_sf"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR035686","properties":[{"key":"EntryName","value":"CPSase_GATase1"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR011059","properties":[{"key":"EntryName","value":"Metal-dep_hydrolase_composite"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00670","properties":[{"key":"EntryName","value":"asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01368","properties":[{"key":"EntryName","value":"CPSaseIIsmall"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002032","properties":[{"key":"EntryName","value":"PRK00856.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009475","properties":[{"key":"EntryName","value":"PRK12838.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF5","properties":[{"key":"EntryName","value":"CAD PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00988","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00185","properties":[{"key":"EntryName","value":"OTCace"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02729","properties":[{"key":"EntryName","value":"OTCace_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00100","properties":[{"key":"EntryName","value":"AOTCASE"}]},{"database":"PRINTS","id":"PR00101","properties":[{"key":"EntryName","value":"ATCASE"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01097","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53671","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52021","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, small subunit N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51338","properties":[{"key":"EntryName","value":"Composite domain of metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00097","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSNIVENSISMSNTTSLQITEVTTVVDSSSSNSGGISSPVIVSNTIINNHRNNNHLSSPRSPTPPVTTSTSSNNTIATLVLKDGSCFQGFSFGAEVKSVSGECVFQTGMVGYPESLTDPSYRGQILVLTFPLIGNYGVPSRDDRDDLTLKKYFESNEIHITGLIIGHYSQDFSHYLAKSSLSDWLKENNIPALYGIDTRALTKKIRTKGVLLGKILFPKSVVGDNLASLPDNKQPWINDYQDVSWVDPNDRNLVAEVSIKEPKLYKPDPTKAIKGSNGKTLRILAVDVGMKFNQIRCFVNRGVEIKIVPWDYDFNQEKDYDGLFISNGPGDPTMVIITIEHLKTALQEAKTPIFGICMGHQLLGIASGAQTIKMKYGNRGHNIPCTDMISGRCYITSQNHGYAVNAKTLSEDFIEFFINANDGSNEGIIHKTLPIFSVQFHPESTPGPRDTEYLFDVFIDSVRESNLTGKLMPIKIPGGTKEENSMKHPRVNVRKVLVLGSGGLSIGQAGEFDYSGSQAIKALKEEGIYTILINPNIATIQTSHSLADKVYFLPVNPDFVRKVIKHEKPDGIYVTFGGQTALSVGIKLKDEFEGLGVKVLGTPIETLIKTEDRELFAQKMLEIEEKCAKSASATNVHEALDAAKEIGYPVICRAAYALGGLGSGFAENEEQLRDICSKAFAISPQVLIERSMKGWKEIEYEVVRDCRDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDFNMLRSTAVNVIRHLGVVGECNIQYALNPFSKEYCIIEVNARLSRSSALASKATGYPLAFVAAKLGLGIPLNEISNSVTKVTCACFEPSLDYVVVKIPRWDLKKFTRVNKSLSSSMKSVGEVMSIGRTFEETIQKAIRAIDFGFLGFSQNDLVDSIDEELVNPSDLRLFAIANALHQGYTVNQIWECTKIDKWFLYKLKNIVELEAKLKKFYHNDITKEIILSAKQLGFSDRQIAKAISSNELAIRRIRQEYGIIPFVKQIDTVAAEFPAHTNYLYVTYNAVEHDINFEERGVMVLGSGVYRIGSSVEFDWCAVRAIRTLREHSIKTITVNYNPETVSTDYDEADRLYFENITLERVLDIYEIERSCGVIISMGGQIPNNIALPLHRQNVKILGTSPEMIDTAENRYKFSRMLDQIGVDQPEWKELTSYDEAHAFCEKVQFPVLVRPSYVLSGAAMNVVYSSDDLSNYLNQATAVSREHPVVISKYIEEAKEIEMDAVALDGKMVMHVISEHVENAGVHSGDATLVLPPQDLDPETVRKIESATQEIGNALNVTGPFNIQFIAKNNDIKVIECNVRASRSFPFVSKVMGVDLIEMATMGMMGLPIEPYPTITLPKNYVAVKVPQFSFSRLSGADPVLGVEMASTGEVACFGRDKYEAYIKALISTGITIPKKNILLSIGSYKEKNEMLPSVQKLHQMGFQLFATSGTADYIQEHGLPVKYLESLDAAEDKLKSEYSLQVHLANNLIDLYINLPSKNKYRRPASYMSKGYKTRRMAVDYDIPLITNVKCAKLFVEALSRRIDFEILNIDYKTSHKRITLPGLINISAFVPHIAEQNSNDFAQVTKASLAAGFTTINVLPIGSTESLQDARTIAIAHSNGKCNAHCDYSLSVAVTESNSLQLTKVVPDAASSFIPFTNLQGATIPKMATISTHFSTWPLLSPIVTDAKGTDLASVLLLANLYDRAVHVTSVSTKEDIVLIALSKEKGLKVTCDVAVYALFLNTNEIQNSEDLLPTPADQVALWEHLDVIDCFTVGTLPYRLAQALNKNNSASTGIEDTIPLLTNAINEGKLTLDDIQKRLYTNPQKIFDIPEQPDTYVEVEIDRKVVIAQKEENWSPFIGKTLVGAVSRVVLRGDTVFLDGGLFSSGNNGKDISTLTHVIAKTPAVKESLSVKESTTQAQQQEVVPAQTSQFVASNIADVMSPPMGPREIRSNSITMDFSELPHSILTTNITSVISHSQFFRKDILTVKDFTRNDLHLLFSVAHEMRTFVERYGSINLLQGRVMFTLFYEPSTRTSASFEAAMNRLGGRVVSIKTDASSVTKGESLGDTIRTVGSYGDIIVLRHPEPGSSKTAAKYSPVPIINAGDGTGEHPTQAFLDVYTIREELGTVNGLTVTLVGDLKNGRTVHSLVRILSQYHVTLNYVSPASLRMPDDVKNEIRKSGIHQREYTDLREVISDTDVLYMTRIQRERFLDLSEYEMVKDAYIINNAILSNSKPQMIVMHPLPRVNEIDPEVDFDDRAAYFRQMRYGMFVRMALLALILGKSS","length":2285,"molWeight":253135,"crc64":"E8552015B7982FBB","md5":"12D8AD674B91DD5B6D436351764B1BA4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":1,"Compositional bias":1,"Active site":3},"uniParcId":"UPI000EBFFBC8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397TMZ6","uniProtkbId":"A0A397TMZ6_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":29,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA99573.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034536"}],"value":"Flavin-containing monooxygenase 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034528"}],"value":"1.14.13.148"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012850"}],"value":"1.14.13.8"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012698"}],"value":"1.6.3.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034561"}],"value":"Dimethylaniline monooxygenase [N-oxide-forming] 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033301"}],"value":"Dimethylaniline monooxygenase [N-oxide-forming] 5"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029725"}],"value":"Dimethylaniline oxidase 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029728"}],"value":"Dimethylaniline oxidase 5"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019213"}],"value":"Flavin-containing monooxygenase 5"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033213"}],"value":"NADPH oxidase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034554"}],"value":"Trimethylamine monooxygenase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA99573.1"}],"value":"C1645_811379"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045722"}],"value":"Acts as a Baeyer-Villiger monooxygenase on a broad range of substrates. Catalyzes the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Active on diverse carbonyl compounds, whereas soft nucleophiles are mostly non- or poorly reactive. In contrast with other forms of FMO it is non- or poorly active on 'classical' substrates such as drugs, pesticides, and dietary components containing soft nucleophilic heteroatoms. Able to oxidize drug molecules bearing a carbonyl group on an aliphatic chain, such as nabumetone and pentoxifylline. Also, in the absence of substrates, shows slow but yet significant NADPH oxidase activity. Acts as a positive modulator of cholesterol biosynthesis as well as glucose homeostasis, promoting metabolic aging via pleiotropic effects"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045957"}],"value":"Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics. Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes. In vitro, catalyzes the N-oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L-carnitine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-geranial + NADPH + O2 + H(+) = (1E)-2,6-dimethylhepta-1,5-dien-1-yl formate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54860"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16980"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:138375"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048989"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54861"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048989"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N,N-dimethylaniline + NADPH + O2 + H(+) = N,N-dimethylaniline N-oxide + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24468"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16269"},{"database":"ChEBI","id":"CHEBI:17735"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.14.13.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049443"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24469"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049443"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047864"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11261"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047864"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"heptan-2-one + NADPH + O2 + H(+) = pentyl acetate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54836"},{"database":"ChEBI","id":"CHEBI:5672"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:87362"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047574"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54837"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047574"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"heptan-4-one + NADPH + O2 + H(+) = propyl butanoate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54852"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:89484"},{"database":"ChEBI","id":"CHEBI:89719"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048990"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54853"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048990"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexan-3-one + NADPH + O2 + H(+) = ethyl butanoate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54844"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:88764"},{"database":"ChEBI","id":"CHEBI:89891"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047977"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54845"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047977"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexan-3-one + NADPH + O2 + H(+) = propyl propanoate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54848"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:89828"},{"database":"ChEBI","id":"CHEBI:89891"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047426"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54849"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047426"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hypotaurine + NADH + O2 + H(+) = taurine + NAD(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:74111"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57853"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:507393"}],"ecNumber":"1.14.13.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047338"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:74112"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047338"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hypotaurine + NADPH + O2 + H(+) = taurine + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:69819"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:57853"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:507393"}],"ecNumber":"1.14.13.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048041"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:69820"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048041"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octan-3-one + NADPH + O2 + H(+) = ethyl hexanoate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54856"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:80946"},{"database":"ChEBI","id":"CHEBI:86055"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048459"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54857"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048459"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octan-3-one + NADPH + O2 + H(+) = pentyl propanoate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54840"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:80946"},{"database":"ChEBI","id":"CHEBI:87373"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049475"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54841"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049475"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sulcatone + NADPH + O2 + H(+) = 4-methylpent-3-en-1-yl acetate + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54864"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16310"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:138373"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047855"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54865"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047855"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"trimethylamine + NADPH + O2 = trimethylamine N-oxide + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31979"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:15724"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:58389"}],"ecNumber":"1.14.13.148","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048088"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:31980"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048088"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004389"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004389"}],"value":"Single-pass membrane protein","id":"SL-9904"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004524"}],"value":"Microsome membrane","id":"SL-0165"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009183"}],"value":"Belongs to the FMO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA99573.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022824"}],"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022481"}],"id":"KW-0488","category":"PTM","name":"Methylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022848"}],"id":"KW-0492","category":"Cellular component","name":"Microsome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023033"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA99573.1"}],"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA99573.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA99573.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000003","properties":[{"key":"ProteinId","value":"RIA99573.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397TMZ6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397TMZ6","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"66881at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005789","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004499","properties":[{"key":"GoTerm","value":"F:N,N-dimethylaniline monooxygenase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016174","properties":[{"key":"GoTerm","value":"F:NAD(P)H oxidase H2O2-forming activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0034899","properties":[{"key":"GoTerm","value":"F:trimethylamine monooxygenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"FunFam","id":"3.50.50.60:FF:000159","properties":[{"key":"EntryName","value":"Dimethylaniline monooxygenase [N-oxide-forming]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.50.60","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036188","properties":[{"key":"EntryName","value":"FAD/NAD-bd_sf"}]},{"database":"InterPro","id":"IPR000960","properties":[{"key":"EntryName","value":"Flavin_mOase"}]},{"database":"InterPro","id":"IPR020946","properties":[{"key":"EntryName","value":"Flavin_mOase-like"}]},{"database":"InterPro","id":"IPR002257","properties":[{"key":"EntryName","value":"Flavin_mOase_5"}]},{"database":"InterPro","id":"IPR050346","properties":[{"key":"EntryName","value":"FMO-like"}]},{"database":"PANTHER","id":"PTHR23023","properties":[{"key":"EntryName","value":"DIMETHYLANILINE MONOOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00743","properties":[{"key":"EntryName","value":"FMO-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000332","properties":[{"key":"EntryName","value":"FMO"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00370","properties":[{"key":"EntryName","value":"FMOXYGENASE"}]},{"database":"PRINTS","id":"PR01125","properties":[{"key":"EntryName","value":"FMOXYGENASE5"}]},{"database":"SUPFAM","id":"SSF51905","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSRVAIIGAGPSGLTSIKQCIDDNLEPVCFEASEHTGGLWRYTEIDDKNEDPHSSIYKSIIIITSKDVMAFTDFPVPYDWPTFLHNSKVAEYFDLYTEKFNLGPYIRFKSPVQRLSIQPDKRWKVTYLNPNNEECEEIFEHVMVCTGHHRYPRLPKYNGMDKFAGKQLHSHFYRRPKDYDNKRVVVVGCGNSGMDIAVELSGIASQVYLCTRKGTLPWILPRRIFGSLPSDHMATRFNIYLPTFMRDLIVKTIAYFTVGPHPTEFAPKTSPSASHPTIKTEFMERVSTGTVIIKPNIAELKDDNSIVFVDGSVISDIDVIIYATGYDIKFPFLDKEIVSGGEKIEQQFEEEYRENLVWLYKYIFPPKLTNIAFIGLVQAIGAIMPVSDLQAQYVTSLWTGNLSSKLPTQSEMEVDIIRNQETLRKRYYHAARHTIEADMVPYMDDLAKDMGCLPDLSKVLLKYGPTLWLQVLFGLPSPMHYRLFGRQAWGGAAEAIRKQNKGSPTMIMCGYPVVIIFGILLGLVLIKLL","length":529,"molWeight":60173,"crc64":"89BA0FF38F062D9E","md5":"9C871BC79E1A6AF24336E219D0B33101"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":13,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"uniParcId":"UPI000EE5932A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397SAS6","uniProtkbId":"A0A397SAS6_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81959.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044985"}],"value":"Lysosomal dipeptide transporter MFSD1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045018"}],"value":"Major facilitator superfamily domain-containing protein 1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81959.1"}],"value":"C1645_700467"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045709"}],"value":"Lysosomal dipeptide uniporter that selectively exports lysine, arginine or histidine-containing dipeptides with a net positive charge from the lysosome lumen into the cytosol. Could play a role in a specific type of protein O-glycosylation indirectly regulating macrophages migration and tissue invasion. Also essential for liver homeostasis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanyl-L-lysine(out) = L-alanyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79415"},{"database":"ChEBI","id":"CHEBI:192470"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044919"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-arginine(out) = L-alpha-aminoacyl-L-arginine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79367"},{"database":"ChEBI","id":"CHEBI:229968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044881"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-histidine(out) = L-alpha-aminoacyl-L-histidine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79375"},{"database":"ChEBI","id":"CHEBI:229967"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044884"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-lysine(out) = L-alpha-aminoacyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79383"},{"database":"ChEBI","id":"CHEBI:229966"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044893"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-L-alpha-amino acid(out) = L-arginyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79371"},{"database":"ChEBI","id":"CHEBI:84315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044899"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-glycine(out) = L-arginyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79391"},{"database":"ChEBI","id":"CHEBI:229955"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-L-lysine(out) = L-aspartyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79411"},{"database":"ChEBI","id":"CHEBI:229953"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044898"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-L-alpha-amino acid(out) = L-histidyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79379"},{"database":"ChEBI","id":"CHEBI:229964"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044912"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-glycine(out) = L-histidyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79395"},{"database":"ChEBI","id":"CHEBI:229957"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044878"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alanine(out) = L-lysyl-L-alanine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79399"},{"database":"ChEBI","id":"CHEBI:229954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044876"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alpha-amino acid(out) = L-lysyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79387"},{"database":"ChEBI","id":"CHEBI:229965"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044891"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-lysine(out) = L-lysyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79403"},{"database":"ChEBI","id":"CHEBI:229956"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044900"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-glycine(out) = L-lysyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79407"},{"database":"ChEBI","id":"CHEBI:191202"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044924"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046376"}],"value":"Homodimer. Interacts with lysosomal protein GLMP (via lumenal domain); the interaction starts while both proteins are still in the endoplasmic reticulum and is required for stabilization of MFSD1 in lysosomes but has no direct effect on its targeting to lysosomes or transporter activity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81959.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":360,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":433,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":445,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":488,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":576,"modifier":"EXACT"},"end":{"value":599,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":515,"modifier":"EXACT"}},"description":"Major facilitator superfamily (MFS) profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50850"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81959.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81959.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000723","properties":[{"key":"ProteinId","value":"RIA81959.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397SAS6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397SAS6","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"424834at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0022857","properties":[{"key":"GoTerm","value":"F:transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.1250.20","properties":[{"key":"EntryName","value":"MFS general substrate transporter like domains"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR011701","properties":[{"key":"EntryName","value":"MFS"}]},{"database":"InterPro","id":"IPR020846","properties":[{"key":"EntryName","value":"MFS_dom"}]},{"database":"InterPro","id":"IPR036259","properties":[{"key":"EntryName","value":"MFS_trans_sf"}]},{"database":"InterPro","id":"IPR052187","properties":[{"key":"EntryName","value":"MFSD1"}]},{"database":"PANTHER","id":"PTHR23512","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23512:SF12","properties":[{"key":"EntryName","value":"TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G00260)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07690","properties":[{"key":"EntryName","value":"MFS_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF103473","properties":[{"key":"EntryName","value":"MFS general substrate transporter"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50850","properties":[{"key":"EntryName","value":"MFS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEQINLTTISTKLSEEEDTDEESDSPSFTPTTLPTSFSTPTVSENSEILDDKEWLIKNKRISTGGSSRRSHHNGEHAGDHLRGQTSGSRRKSLKVDNADHIIKMCAMACACTFGVGSHFASHIIGPMKGILMEQLDLTNTQFSLLVASLTLCNTVIPIVSGLLVARFGTTRSSLVITTIILLGMIIFTAASWNGKVGLMIAGFIVFGMGLAPLTIVQETIIVQFFQGNGLGFALAVGLTLGRLASFVATVLAVPLSLMEPLTYRTPFIVATATCAVSWIMNIVYVYILKHADNRKNHNKEGVALHSVVEKKAVHWNAIFDLSDIFWWFLVVGILFGASMSPFLHLSSNIIKHRFDTTDMLAAWDSSVILLLPVILYPFLGLFLDKFGFRFISITYLLLLSPPNLIHPFPPIFLFAVAYAAVPLTMVTLIPLLTKNVSTGLGLLKSVDNIGATLSQTFAGILLDEHVRHKKYIIDDEGIEYGHEDDDLVALRMFAILSSFLFLVSLVFWWMDKTYKGGSLNAKYEGEYHNDNTNNYGQLRSSDDDDEVHSAGLMRMIVIEEEISFVRDESIKKRKRTIIYMGILGLMMIICWIVFGVVAFEKAGISASDEKVSE","length":613,"molWeight":67810,"crc64":"3933B6A72ABC1F83","md5":"AB7E2B5374D15710AA2FE372776AF530"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":13,"Domain":1,"Region":2,"Compositional bias":4},"uniParcId":"UPI000ECF18F9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397SET4","uniProtkbId":"A0A397SET4_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":21,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA83236.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase proenzyme 2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"4.1.1.65"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase 2 beta chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase 2 alpha chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"PSD2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA83236.1"}],"value":"C1645_699640"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20828"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57262"},{"database":"ChEBI","id":"CHEBI:64612"}],"ecNumber":"4.1.1.65","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Binds 1 pyruvoyl group covalently per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Golgi apparatus membrane","id":"SL-0134"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Endosome membrane","id":"SL-0100"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA83236.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":765,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 2 beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"featureId":"PRO_5023415536"},{"type":"Chain","location":{"start":{"value":766,"modifier":"EXACT"},"end":{"value":798,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 2 alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"featureId":"PRO_5023415537"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Domain","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Domain","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"EF-hand","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50222"}]},{"type":"Active site","location":{"start":{"value":623,"modifier":"EXACT"},"end":{"value":623,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":679,"modifier":"EXACT"},"end":{"value":679,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":766,"modifier":"EXACT"},"end":{"value":766,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":766,"modifier":"EXACT"},"end":{"value":766,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Site","location":{"start":{"value":765,"modifier":"EXACT"},"end":{"value":766,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Modified residue","location":{"start":{"value":766,"modifier":"EXACT"},"end":{"value":766,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10142"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0967","category":"Cellular component","name":"Endosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0333","category":"Cellular component","name":"Golgi apparatus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10142"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023264"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023317"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA83236.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA83236.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000588","properties":[{"key":"ProteinId","value":"RIA83236.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397SET4","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397SET4","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"5973539at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00558","properties":[{"key":"RectionId","value":"UER00616"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0010008","properties":[{"key":"GoTerm","value":"C:endosome membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000139","properties":[{"key":"GoTerm","value":"C:Golgi membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005795","properties":[{"key":"GoTerm","value":"C:Golgi stack"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005509","properties":[{"key":"GoTerm","value":"F:calcium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004609","properties":[{"key":"GoTerm","value":"F:phosphatidylserine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006646","properties":[{"key":"GoTerm","value":"P:phosphatidylethanolamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016540","properties":[{"key":"GoTerm","value":"P:protein autoprocessing"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"2.60.40.150","properties":[{"key":"EntryName","value":"C2 domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.238.10","properties":[{"key":"EntryName","value":"EF-hand"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00663","properties":[{"key":"EntryName","value":"PS_decarb_PSD_B_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000008","properties":[{"key":"EntryName","value":"C2_dom"}]},{"database":"InterPro","id":"IPR035892","properties":[{"key":"EntryName","value":"C2_domain_sf"}]},{"database":"InterPro","id":"IPR011992","properties":[{"key":"EntryName","value":"EF-hand-dom_pair"}]},{"database":"InterPro","id":"IPR018247","properties":[{"key":"EntryName","value":"EF_Hand_1_Ca_BS"}]},{"database":"InterPro","id":"IPR002048","properties":[{"key":"EntryName","value":"EF_hand_dom"}]},{"database":"InterPro","id":"IPR003817","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"}]},{"database":"InterPro","id":"IPR033177","properties":[{"key":"EntryName","value":"PSD-B"}]},{"database":"InterPro","id":"IPR033179","properties":[{"key":"EntryName","value":"PSD_type2_pro"}]},{"database":"NCBIfam","id":"TIGR00163","properties":[{"key":"EntryName","value":"PS_decarb"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067:SF17","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00168","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02666","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00239","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF49562","properties":[{"key":"EntryName","value":"C2 domain (Calcium/lipid-binding domain, CaLB)"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF47473","properties":[{"key":"EntryName","value":"EF-hand"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50004","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00018","properties":[{"key":"EntryName","value":"EF_HAND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50222","properties":[{"key":"EntryName","value":"EF_HAND_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSELNVILRINVIEAKNLAAKDRNGFSDPFVTINIDDSTYQTHVVNKNLNPKWDAIFDHKVDLNKSPSEIHFTCWDKDVFGRDYLGEIFVSLDKLWENNGHISFDDEFNLPQWYSLTTTRKNEDVSGQILIKIGLRDKDNKSLDAREWNSIWRKMNNLSINEEQSQPAASSTVRPSHERHSSLSTLSDIVGVIFLEIVCAIDLPAERNMTGLGFDMDPFVIVSFAKNTFRTKIINHNLNPEWNEKLHFSVKKQECDFQIKFSIYDWDKFSQNDHIASKLYDVRPLIERGIASMKSAREFDNMEDGLLEEVLTLEVHSKLANKHDSKLVIRTKFIPYEQLRKQFWYALAKFYDSDGNNLLNYVELETMLQSLGSTLSQETINSFYTRFGKDPKRHALKFDELVSCLEQYLGDASFSHHSANLDGEEADNEHLIYLQNCPICNRPNLDQLTETNIITHVAMCASSDWGNIDKFVTGDFVTESQAQRKWVSKVITKVGFGGYKIGGNNANIIVQDRKSGQLVEEKMAAYVRLGIRLLYRGVGSIDSASAKKLLESMSIKQGKKFNHPSSVADIKPFIKFHKLNIDEIADPLDSFKNFNEFFYRKLKPGARPCDSPQDPHVLVSPADCRMMAFPTVTKATELWIKGQSFSIARLLDDDLIAKEYEGGSLGIFRLAPQDYHRFHFPVEGELGPVKDIPGAYFTVNPMAIRSPLDVYGENKRAVCYINSPQFGKVAYITIGAMMVGSILFTSTPKSYVRRTDEHGYFAFGGSTVILLFQKGKMIWDEDLLANSKTCLETLVSIQ","length":798,"molWeight":90832,"crc64":"A20608C360D316D6","md5":"E7AC9E16E683A21AF615B60AD41359D4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":2,"Domain":3,"Active site":4,"Site":1,"Modified residue":1},"uniParcId":"UPI000EE1B179"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397SJD8","uniProtkbId":"A0A397SJD8_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-12-05","entryVersion":22,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA84097.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039850"}],"value":"Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012046"}],"value":"1.3.8.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039036"}],"value":"1.3.8.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042821"}],"value":"2-methyl branched chain acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00041537"}],"value":"2-methylbutyryl-coenzyme A dehydrogenase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA84097.1"}],"value":"C1645_784848"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094237"}],"value":"Short and branched chain specific acyl-CoA dehydrogenase that catalyzes the proR-proR stereospecific alpha,beta-dehydrogenation of fatty acyl-CoA thioesters using the electron transfer flavoprotein (ETF) as their physiologic electron acceptor, resulting in the formation of trans-2-enoyl-CoA ((2E)-enoyl-CoA). Among the different mitochondrial acyl-CoA dehydrogenases, acts specifically on short and branched chain acyl-CoA derivatives such as (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such as butyryl-CoA (butanoyl-CoA). Plays an important role in the metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic pathway. Can also act on valproyl-CoA, a metabolite of valproic acid, an antiepileptic drug"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = ethylacryloyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65296"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:156439"},{"database":"ChEBI","id":"CHEBI:156440"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048592"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65297"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048592"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2S)-2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48256"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57337"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:88166"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049552"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:48257"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049552"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43780"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57336"},{"database":"ChEBI","id":"CHEBI:57337"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"ecNumber":"1.3.8.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048235"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:43781"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048235"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylpropanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = 2-methylpropenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44180"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57338"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62500"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051903"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:44181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051903"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a short-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47196"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:87487"},{"database":"ChEBI","id":"CHEBI:87488"}],"ecNumber":"1.3.8.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051002"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:47197"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051002"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"butanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24004"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:57371"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049096"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24005"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049096"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43464"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62077"},{"database":"ChEBI","id":"CHEBI:62620"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049192"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:43465"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049192"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"valproyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-propylpent-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65344"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:156457"},{"database":"ChEBI","id":"CHEBI:156458"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048307"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65345"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048307"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00037895"}],"value":"Amino-acid degradation; L-isoleucine degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005198"}],"value":"Lipid metabolism; mitochondrial fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004305"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"value":"Belongs to the acyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA84097.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02771"}]},{"type":"Domain","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA84097.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA84097.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000517","properties":[{"key":"ProteinId","value":"RIA84097.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397SJD8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397SJD8","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"10262177at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003853","properties":[{"key":"GoTerm","value":"F:short-chain 2-methyl fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046395","properties":[{"key":"GoTerm","value":"P:carboxylic acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006631","properties":[{"key":"GoTerm","value":"P:fatty acid metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd01158","properties":[{"key":"EntryName","value":"SCAD_SBCAD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.540.10:FF:000012","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase short/branched chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.140.10:FF:000002","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase short/branched chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.110.10:FF:000001","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.540.10","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase/oxidase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.140.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006089","properties":[{"key":"EntryName","value":"Acyl-CoA_DH_CS"}]},{"database":"InterPro","id":"IPR046373","properties":[{"key":"EntryName","value":"Acyl-CoA_Oxase/DH_mid-dom_sf"}]},{"database":"InterPro","id":"IPR036250","properties":[{"key":"EntryName","value":"AcylCo_DH-like_C"}]},{"database":"InterPro","id":"IPR009075","properties":[{"key":"EntryName","value":"AcylCo_DH/oxidase_C"}]},{"database":"InterPro","id":"IPR006091","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_M"}]},{"database":"InterPro","id":"IPR013786","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N"}]},{"database":"InterPro","id":"IPR037069","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N_sf"}]},{"database":"InterPro","id":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"PANTHER","id":"PTHR43884","properties":[{"key":"EntryName","value":"ACYL-COA DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43884:SF1","properties":[{"key":"EntryName","value":"SHORT_BRANCHED CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02771","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47203","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56645","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase NM domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00072","properties":[{"key":"EntryName","value":"ACYL_COA_DH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00073","properties":[{"key":"EntryName","value":"ACYL_COA_DH_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSFVSIARNKFSLAFRQNISSFTSFNSRFARPKQGAFSRYASTLSSLNTLSEEEESIRNSVASFAHQKIQPLVAKMDEKEYVEPEIIKGLFEQGLMGIETETEYGGTGSGFLAAILVVEELAKVDPSISVICDVQNTLVNTLLRKYGNDFVKEKYLPQLATEKVGCFCLSESGAGSDAFALKTRADKKDGYYILNGSKMWITNSKEAEIFLVFANLDPSKGYKGITCFILEKDMGVQIAKKESKLGIRASSTCTLNFDDVKVPEENVLGEIGKGYKYAIEILNEGRIGIAAQMIGLSQGVYDYALAYMFQRKAFNKLIGEFQGMQHQYAQVATEIEAARLLTYNAARLKEEGKDFIKEAAMAKLYASQVAEKTASKAIEWMGGVGFTREFPVEKFYRDAKIGSIYEGTSNIQLTTIAKLIAHKFK","length":425,"molWeight":47170,"crc64":"B7E85F8C1001710C","md5":"1DA11DA96D376AFCCC2364B93AF4021A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":8,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI000EB8ACCE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397T2B7","uniProtkbId":"A0A397T2B7_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-12-05","entryVersion":28,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA89301.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Lon protease homolog, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"3.4.21.53"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"PIM1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA89301.1"}],"value":"C1645_825066"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of proteins in presence of ATP.","ecNumber":"3.4.21.53","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10087"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Homohexamer or homoheptamer. Organized in a ring with a central cavity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004305"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000591"}],"value":"Belongs to the peptidase S16 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA89301.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":468,"modifier":"EXACT"}},"description":"Lon N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51787"}]},{"type":"Domain","location":{"start":{"value":900,"modifier":"EXACT"},"end":{"value":1086,"modifier":"EXACT"}},"description":"Lon proteolytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51786"}]},{"type":"Region","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":836,"modifier":"EXACT"},"end":{"value":868,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":836,"modifier":"EXACT"},"end":{"value":848,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":850,"modifier":"EXACT"},"end":{"value":868,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":992,"modifier":"EXACT"},"end":{"value":992,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10087"}]},{"type":"Active site","location":{"start":{"value":1035,"modifier":"EXACT"},"end":{"value":1035,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"}]},{"type":"Binding site","location":{"start":{"value":621,"modifier":"EXACT"},"end":{"value":628,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA89301.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA89301.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000225","properties":[{"key":"ProteinId","value":"RIA89301.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397T2B7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397T2B7","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"2411602at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043565","properties":[{"key":"GoTerm","value":"F:sequence-specific DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003697","properties":[{"key":"GoTerm","value":"F:single-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0034599","properties":[{"key":"GoTerm","value":"P:cellular response to oxidative stress"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051131","properties":[{"key":"GoTerm","value":"P:chaperone-mediated protein complex assembly"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0007005","properties":[{"key":"GoTerm","value":"P:mitochondrion organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0070407","properties":[{"key":"GoTerm","value":"P:oxidation-dependent protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19500","properties":[{"key":"EntryName","value":"RecA-like_Lon"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000021","properties":[{"key":"EntryName","value":"Lon protease homolog"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000113","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.5.5270:FF:000001","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.1480:FF:000003","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.30.130.40:FF:000010","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.230.10:FF:000015","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.5270","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.1480","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.130.40","properties":[{"key":"EntryName","value":"LON domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03120","properties":[{"key":"EntryName","value":"lonm_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR004815","properties":[{"key":"EntryName","value":"Lon_bac/euk-typ"}]},{"database":"InterPro","id":"IPR054594","properties":[{"key":"EntryName","value":"Lon_lid"}]},{"database":"InterPro","id":"IPR008269","properties":[{"key":"EntryName","value":"Lon_proteolytic"}]},{"database":"InterPro","id":"IPR027065","properties":[{"key":"EntryName","value":"Lon_Prtase"}]},{"database":"InterPro","id":"IPR003111","properties":[{"key":"EntryName","value":"Lon_prtase_N"}]},{"database":"InterPro","id":"IPR046336","properties":[{"key":"EntryName","value":"Lon_prtase_N_sf"}]},{"database":"InterPro","id":"IPR027503","properties":[{"key":"EntryName","value":"Lonm_euk"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR008268","properties":[{"key":"EntryName","value":"Peptidase_S16_AS"}]},{"database":"InterPro","id":"IPR015947","properties":[{"key":"EntryName","value":"PUA-like_sf"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"InterPro","id":"IPR014721","properties":[{"key":"EntryName","value":"Ribsml_uS5_D2-typ_fold_subgr"}]},{"database":"NCBIfam","id":"TIGR00763","properties":[{"key":"EntryName","value":"lon"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43718","properties":[{"key":"EntryName","value":"LON PROTEASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43718:SF2","properties":[{"key":"EntryName","value":"LON PROTEASE HOMOLOG, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05362","properties":[{"key":"EntryName","value":"Lon_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22667","properties":[{"key":"EntryName","value":"Lon_lid"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02190","properties":[{"key":"EntryName","value":"LON_substr_bdg"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00830","properties":[{"key":"EntryName","value":"ENDOLAPTASE"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00464","properties":[{"key":"EntryName","value":"LON"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88697","properties":[{"key":"EntryName","value":"PUA domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51787","properties":[{"key":"EntryName","value":"LON_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51786","properties":[{"key":"EntryName","value":"LON_PROTEOLYTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01046","properties":[{"key":"EntryName","value":"LON_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAYIRNCLQINFTGGAFARSPITFIKSTITLGSRKFSNQSSSYIPRSNLSKFLSHSVPHTSAYSNSPILLLLQPLRNETQYQRTFSCNTSQQFLFFTRSYSRGKSKSNESKLNSDGDNDSKENGSKGGGQQGEGGENSNGNNGDSSSNGNNGENPNNGNKGNGNKGNNGSNKNSGDGSGDGSAPRSPFEGIHRTLQVLETTLQKPSIPEVYPQVLAIPITRRPLFPGFYKAVVIKDPHVTASVKELMKRGQPYVGAFLLRDEEADVDIITDISQVYRVGVFAQITSVFPANGGQDENSLTAVLYPHRRIRIKELLPPLPSGVSEAEVVSDSVQQTAVEETTPPNLTSPRPKETQYATSFLEDYNVSLVNVENLNDESYNRKNQIVRAITSEIVAVFKDIATLNPLFRDQIANFSMSQSAGNVFEEPAKLADFAAAVSTGEPHELQEVLESLVIEERLQKALLVLKKELVNAQLQSKISKEVESKIAKRQREYYLMEQLKGIKKELGIESDGKDKLVEKFKEKADKLEMPEGVKKVFEEEINKLAHLEPAASEFNVTRNYLDWLTQVPWGLRSPENYNIKHAVKVLDEDHYGLQDVKDRILEFIAVGKLRGTVEGKILCFVGPPGVGKTSIGKSIARALSRQFYRFSVGGLTDVAEIKGHRRTYVGAMPGKVVQALKKVQTENPLVLIDEVDKIGRGHQGDPASALLELLDPEQNSSFLDHYMDVPIDLSKVLFVCTANVVDTIPGPLLDRMEVIQLSGYVADEKVAIASKYLAPTAKTMAGLQNADVNLQQDAIEVLIKSYCRESGVRNLKKHIDKIYRKAALKIVRDIGDEEFPSQELDNVETESETSESSKEKDESSITTEPRKPLEIPADVHMNISPENLKDYVGPPLWHSDRLYDVTPPGVAMGLAWTSMGGSALYIESTLESILTPTSSPSLSKTGQMGDVMKESSDIAYTFAKSLMVRSYPENKFFERAAIHLHVPEGATPKDGPSAGITMATSLLSLAFNKSLDPTIAMTGELTLTGKVLKIGGLREKAVAAKRSGVTTLIYPDANISDWEELPDNIKDGLNGIPVGWYDDVFKVVFKDITKEDAAKTWLEMIKLDSKVPKVDNKKENIGIFVDSEKEKVIDVARLLN","length":1135,"molWeight":125029,"crc64":"0A2A4D9580D48233","md5":"339EE7117C6605E995618CC4F251D003"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Compositional bias":5,"Active site":2,"Binding site":1},"uniParcId":"UPI000EC00007"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397T5M1","uniProtkbId":"A0A397T5M1_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":30,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92216.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022255"}],"value":"Histone acetyltransferase ESA1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"2.3.1.48"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074445"}],"value":"Histone acetyltransferase esa1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031065"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075313"}],"value":"protein 2-hydroxyisobutyryltransferase ESA1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031553"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00076782"}],"value":"protein acetyltransferase ESA1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031133"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077673"}],"value":"protein crotonyltransferase ESA1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92216.1"}],"value":"C1645_723574"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53908"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:13707"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:137954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53909"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24180"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:15921"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:131780"},{"database":"ChEBI","id":"CHEBI:144968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21992"},{"database":"Rhea","id":"RHEA-COMP:9845"},{"database":"Rhea","id":"RHEA-COMP:11338"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21993"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:45949"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010107"}],"value":"Belongs to the MYST (SAS/MOZ) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92216.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"MYST-type HAT","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51726"}]},{"type":"Active site","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602717-51"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]},{"type":"Binding site","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":439,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Modified residue","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023159"}],"id":"KW-0010","category":"Molecular function","name":"Activator"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92216.1"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022853"}],"id":"KW-0156","category":"Molecular function","name":"Chromatin regulator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92216.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92216.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000132","properties":[{"key":"ProteinId","value":"RIA92216.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397T5M1","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397T5M1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"787137at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0035267","properties":[{"key":"GoTerm","value":"C:NuA4 histone acetyltransferase complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003682","properties":[{"key":"GoTerm","value":"F:chromatin binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010485","properties":[{"key":"GoTerm","value":"F:histone H4 acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0106226","properties":[{"key":"GoTerm","value":"F:peptide 2-hydroxyisobutyryltransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0140064","properties":[{"key":"GoTerm","value":"F:peptide crotonyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0003712","properties":[{"key":"GoTerm","value":"F:transcription coregulator activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006974","properties":[{"key":"GoTerm","value":"P:DNA damage response"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006357","properties":[{"key":"GoTerm","value":"P:regulation of transcription by RNA polymerase II"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"FunFam","id":"1.10.10.10:FF:000526","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.60.60:FF:000001","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.630.30:FF:000001","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.30.140","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.60.60","properties":[{"key":"EntryName","value":"N-acetyl transferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016181","properties":[{"key":"EntryName","value":"Acyl_CoA_acyltransferase"}]},{"database":"InterPro","id":"IPR016197","properties":[{"key":"EntryName","value":"Chromo-like_dom_sf"}]},{"database":"InterPro","id":"IPR000953","properties":[{"key":"EntryName","value":"Chromo/chromo_shadow_dom"}]},{"database":"InterPro","id":"IPR002717","properties":[{"key":"EntryName","value":"HAT_MYST-type"}]},{"database":"InterPro","id":"IPR050603","properties":[{"key":"EntryName","value":"MYST_HAT"}]},{"database":"InterPro","id":"IPR025995","properties":[{"key":"EntryName","value":"Tudor-knot"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR040706","properties":[{"key":"EntryName","value":"Zf-MYST"}]},{"database":"PANTHER","id":"PTHR10615","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10615:SF218","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE ESA1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01853","properties":[{"key":"EntryName","value":"MOZ_SAS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11717","properties":[{"key":"EntryName","value":"Tudor-knot"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17772","properties":[{"key":"EntryName","value":"zf-MYST"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00298","properties":[{"key":"EntryName","value":"CHROMO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55729","properties":[{"key":"EntryName","value":"Acyl-CoA N-acyltransferases (Nat)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54160","properties":[{"key":"EntryName","value":"Chromo domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51726","properties":[{"key":"EntryName","value":"MYST_HAT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MESDTNSISVEHESIPITPVQTSTTEVIENEIIIGNKYYVRLENHADSEEEIQYRIGEILSNRTNYEGNQEYYVHFVDFNKRLDEWVPEDRIDTKIDVIFEKPKLTTPKKANLSLEDPSTPPTASTALKMTYGYSTPPVTLTAFESPGSIGSVTSTSFMNEETTKGEAVGAMSCRPNKRRVKNLQEIHFGEFSIETWYFSPYPEEFNDSPIIYICEFCLSYFISEFQLRRHVSKCTVMHPPGNEIYRDEEISFFEIDGARQPTYCQNLCLLSKLFLDHKSLTYDLLPFLFYIMCKQDQYGYHIIGYFSKEKNYTLNNLACILTLPPYQRKGYGRLLISFSYELSKIEGRIGSPERPLSDLGLLSYQQYWYETILEVLWDTKEIGDDYISIDEITAKTSITQSDVLFTLYESGICVYQGQICIRLTEAMLDTSLNSISKKRRINIENLKWSPPHFTANQLRYKN","length":463,"molWeight":53643,"crc64":"774C5C87226AE6B4","md5":"56A847C84D224A2BB29FC60D3C3E0430"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":5,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":2,"Modified residue":1},"uniParcId":"UPI000EC9DE92"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397TAN8","uniProtkbId":"A0A397TAN8_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-12-05","entryVersion":22,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92061.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Phosphohexokinase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92061.1"}],"value":"C1645_766023"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16109"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade \"E\" sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92061.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":501,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Domain","location":{"start":{"value":581,"modifier":"EXACT"},"end":{"value":871,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":567,"modifier":"EXACT"}},"description":"N-terminal catalytic PFK domain 1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Region","location":{"start":{"value":581,"modifier":"EXACT"},"end":{"value":952,"modifier":"EXACT"}},"description":"C-terminal regulatory PFK domain 2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Active site","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Binding site","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":442,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":469,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":475,"modifier":"EXACT"},"end":{"value":478,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":650,"modifier":"EXACT"},"end":{"value":650,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":708,"modifier":"EXACT"},"end":{"value":712,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":746,"modifier":"EXACT"},"end":{"value":746,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":753,"modifier":"EXACT"},"end":{"value":755,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":813,"modifier":"EXACT"},"end":{"value":813,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":839,"modifier":"EXACT"},"end":{"value":839,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":845,"modifier":"EXACT"},"end":{"value":848,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":923,"modifier":"EXACT"},"end":{"value":923,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92061.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA92061.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000136","properties":[{"key":"ProteinId","value":"RIA92061.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397TAN8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397TAN8","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"537915at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.40.50.460:FF:000007","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.460:FF:000008","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.10.180.10","properties":[{"key":"EntryName","value":"2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_03184","properties":[{"key":"EntryName","value":"Phosphofructokinase_I_E"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009161","properties":[{"key":"EntryName","value":"6-Pfructokinase_euk"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR029068","properties":[{"key":"EntryName","value":"Glyas_Bleomycin-R_OHBP_Dase"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02478","properties":[{"key":"EntryName","value":"6PF1K_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF4","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"2"}]},{"database":"PIRSF","id":"PIRSF000533","properties":[{"key":"EntryName","value":"ATP_PFK_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSIIEGLSHIVLIASSIEKYENSVQFYSLFGYQTISHFVNSKVPTNEVQFLPQEEKLLHLFGKPPTKDITLKIVLATNTNEKEPFPEEKDWRLEQASLVSVTNDIVAVESILKSINIRYQKYTYPDVNESDLLATPPPADFVHTEVYTHDPLNNLITFTNKPNPFSKSIYPIKPKSPVQQDIDISTQPKVERKRIGVLTSGGDSPGMNAAVRAIVRVAISRGCDAYAIFEGYEGLVNGGDMIKKFGWADVRGYLAIGGTLIGTARCASFRERKGRLSAAYNLIKNGIDALIVCGGDGSLTGADVLRSEWPGLLEDLIKEGRITIEEATRFKHLTVVGLVGSIDNDMSSTDITIGAVTSLHRICEAIDSISSTALSHSRAFVIEVMGRHCGWLALMAAVSTGADFVFIPERPPISDDWESEMCETLKKHRDLGKRMTIVIVAEGAIDKNLDPIRPEYIKKLLTDHGLDTRVTTLGHTQRGGKPCSFDRNLATIQGVEAVQAVLRATPDTPSPMIGIRENKITCEPLMKAVELTRQVAEAIAQKDFRRAMDLRDPEFSEDYQAYIDLAVVNEKLSLRENQCLRLGIIHIGAPAGGMNSATRAAVRYALNHGHIPVAIYNGFDGLLQDNLRELSWIDVDGWAGKGGSELGTNKINISELDVGMIAYQLQKHRINSLLLIGGFEAYTSLIELNRSRNQYPAFCIPMVCLPATISNNVPGTDFSLGSDTSLNAIVDSCDSIKQSASASRRRVFVVEVQGGHCGYLAVLAGLAVGATSAYIPEEGVSLKKLQADLNHLTRRFGEDKKGTSSGRLFLRNECVSNTYTTDVIASIFKSESRGLYDSRTSILGHIQQGGTPSPTDRIRATRLAVKCIKFLEQYALPPTSEKIVYPSIYTNVKESAAVIGIEGAQVIFTPVIDLLSETDMKNRKSTKTWWIHLKELVEILSKWGKITFFKKI","length":952,"molWeight":104784,"crc64":"967E893B4655B1BF","md5":"EC13B723B7B42A06AFF41CD1EEDE8BB6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":18},"uniParcId":"UPI000EE7D891"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397TGW4","uniProtkbId":"A0A397TGW4_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":33,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA96599.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"histone acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"2.3.1.48"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA96599.1"}],"value":"C1645_754678"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045805"}],"value":"Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination. Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53908"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:13707"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:137954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53909"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24180"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:15921"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:131780"},{"database":"ChEBI","id":"CHEBI:144968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21992"},{"database":"Rhea","id":"RHEA-COMP:9845"},{"database":"Rhea","id":"RHEA-COMP:11338"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21993"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:45949"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004286"}],"value":"Chromosome","id":"SL-0468"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010107"}],"value":"Belongs to the MYST (SAS/MOZ) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA96599.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":484,"modifier":"EXACT"}},"description":"MYST-type HAT","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51726"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602717-51"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]},{"type":"Binding site","location":{"start":{"value":389,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":398,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Modified residue","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023159"}],"id":"KW-0010","category":"Molecular function","name":"Activator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022853"}],"id":"KW-0156","category":"Molecular function","name":"Chromatin regulator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022454"}],"id":"KW-0158","category":"Cellular component","name":"Chromosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA96599.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA96599.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000043","properties":[{"key":"ProteinId","value":"RIA96599.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397TGW4","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397TGW4","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"787137at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0000785","properties":[{"key":"GoTerm","value":"C:chromatin"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0032991","properties":[{"key":"GoTerm","value":"C:protein-containing complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0003682","properties":[{"key":"GoTerm","value":"F:chromatin binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004402","properties":[{"key":"GoTerm","value":"F:histone acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0106226","properties":[{"key":"GoTerm","value":"F:peptide 2-hydroxyisobutyryltransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0140064","properties":[{"key":"GoTerm","value":"F:peptide crotonyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0003712","properties":[{"key":"GoTerm","value":"F:transcription coregulator activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0033554","properties":[{"key":"GoTerm","value":"P:cellular response to stress"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006357","properties":[{"key":"GoTerm","value":"P:regulation of transcription by RNA polymerase II"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04301","properties":[{"key":"EntryName","value":"NAT_SF"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.10.10:FF:000022","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.30.30.140:FF:000013","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.60.60:FF:000001","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.630.30:FF:000002","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.30.140","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.60.60","properties":[{"key":"EntryName","value":"N-acetyl transferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016181","properties":[{"key":"EntryName","value":"Acyl_CoA_acyltransferase"}]},{"database":"InterPro","id":"IPR016197","properties":[{"key":"EntryName","value":"Chromo-like_dom_sf"}]},{"database":"InterPro","id":"IPR000953","properties":[{"key":"EntryName","value":"Chromo/chromo_shadow_dom"}]},{"database":"InterPro","id":"IPR002717","properties":[{"key":"EntryName","value":"HAT_MYST-type"}]},{"database":"InterPro","id":"IPR050603","properties":[{"key":"EntryName","value":"MYST_HAT"}]},{"database":"InterPro","id":"IPR025995","properties":[{"key":"EntryName","value":"Tudor-knot"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR040706","properties":[{"key":"EntryName","value":"Zf-MYST"}]},{"database":"PANTHER","id":"PTHR10615","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10615:SF218","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE ESA1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01853","properties":[{"key":"EntryName","value":"MOZ_SAS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11717","properties":[{"key":"EntryName","value":"Tudor-knot"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17772","properties":[{"key":"EntryName","value":"zf-MYST"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00298","properties":[{"key":"EntryName","value":"CHROMO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55729","properties":[{"key":"EntryName","value":"Acyl-CoA N-acyltransferases (Nat)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54160","properties":[{"key":"EntryName","value":"Chromo domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51726","properties":[{"key":"EntryName","value":"MYST_HAT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTQRFSASPSPRPGTPTHRASTPGAEVVVGCKVFVEVKKEKKDETQEFRKAEILSVRTHNEKTEYYVHFVEFNKRLDEWVGLERIDFTKEIERPAKKRNGKGGNQFRDSDTPSRVGSPLREVTGRSSGVGSTVGQKRKISALEDTPTPNAKATTPSTPLVETTGEDYEDGGTPGNGTPLGPLAATFSKEQEIERLRTSGSMTQSHSEISRVKNLERIHFGEYDVDTWYFSPYPQEYSDAAVVYICEFCLFHYISERQLRRHLQKCTVRHPPGNEIYRCDDISFFEIDGNKQKTYCRNLCLLSKLFLDHKTLYYDVDPFLFYIMCQQDEFGCHMIGYFSKEKESTEGYNLACILTLPQHQRKGFGRLLIAFSYELSKKEGKVGSPEKPLSDLGLLSYRSYWTEVIVELLLETKEINEDITIEDISARTSIATTDILQTLQSLCAIKPYKGQQILCLSDGVIASYHKTKEKHKNRRIDESCLQWTPPHFTSNQLRYI","length":495,"molWeight":56578,"crc64":"7B859F7195EAC2D7","md5":"62A135DFAC8663DEF4CBF09CB3053741"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":2,"Active site":1,"Binding site":2,"Modified residue":1},"uniParcId":"UPI000ED2E7FA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397TIC9","uniProtkbId":"A0A397TIC9_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-12-05","entryVersion":21,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA97990.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044985"}],"value":"Lysosomal dipeptide transporter MFSD1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045018"}],"value":"Major facilitator superfamily domain-containing protein 1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA97990.1"}],"value":"C1645_870977"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045709"}],"value":"Lysosomal dipeptide uniporter that selectively exports lysine, arginine or histidine-containing dipeptides with a net positive charge from the lysosome lumen into the cytosol. Could play a role in a specific type of protein O-glycosylation indirectly regulating macrophages migration and tissue invasion. Also essential for liver homeostasis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanyl-L-lysine(out) = L-alanyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79415"},{"database":"ChEBI","id":"CHEBI:192470"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044919"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-arginine(out) = L-alpha-aminoacyl-L-arginine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79367"},{"database":"ChEBI","id":"CHEBI:229968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044881"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-histidine(out) = L-alpha-aminoacyl-L-histidine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79375"},{"database":"ChEBI","id":"CHEBI:229967"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044884"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-lysine(out) = L-alpha-aminoacyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79383"},{"database":"ChEBI","id":"CHEBI:229966"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044893"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-L-alpha-amino acid(out) = L-arginyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79371"},{"database":"ChEBI","id":"CHEBI:84315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044899"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-glycine(out) = L-arginyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79391"},{"database":"ChEBI","id":"CHEBI:229955"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-L-lysine(out) = L-aspartyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79411"},{"database":"ChEBI","id":"CHEBI:229953"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044898"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-L-alpha-amino acid(out) = L-histidyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79379"},{"database":"ChEBI","id":"CHEBI:229964"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044912"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-glycine(out) = L-histidyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79395"},{"database":"ChEBI","id":"CHEBI:229957"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044878"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alanine(out) = L-lysyl-L-alanine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79399"},{"database":"ChEBI","id":"CHEBI:229954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044876"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alpha-amino acid(out) = L-lysyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79387"},{"database":"ChEBI","id":"CHEBI:229965"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044891"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-lysine(out) = L-lysyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79403"},{"database":"ChEBI","id":"CHEBI:229956"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044900"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-glycine(out) = L-lysyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79407"},{"database":"ChEBI","id":"CHEBI:191202"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044924"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046376"}],"value":"Homodimer. Interacts with lysosomal protein GLMP (via lumenal domain); the interaction starts while both proteins are still in the endoplasmic reticulum and is required for stabilization of MFSD1 in lysosomes but has no direct effect on its targeting to lysosomes or transporter activity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA97990.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":441,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":453,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":532,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":479,"modifier":"EXACT"}},"description":"Major facilitator superfamily (MFS) profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50850"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA97990.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA97990.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000022","properties":[{"key":"ProteinId","value":"RIA97990.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397TIC9","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397TIC9","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"424834at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0022857","properties":[{"key":"GoTerm","value":"F:transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.1250.20","properties":[{"key":"EntryName","value":"MFS general substrate transporter like domains"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR011701","properties":[{"key":"EntryName","value":"MFS"}]},{"database":"InterPro","id":"IPR020846","properties":[{"key":"EntryName","value":"MFS_dom"}]},{"database":"InterPro","id":"IPR036259","properties":[{"key":"EntryName","value":"MFS_trans_sf"}]},{"database":"InterPro","id":"IPR052187","properties":[{"key":"EntryName","value":"MFSD1"}]},{"database":"PANTHER","id":"PTHR23512","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23512:SF12","properties":[{"key":"EntryName","value":"TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G00260)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07690","properties":[{"key":"EntryName","value":"MFS_1"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF103473","properties":[{"key":"EntryName","value":"MFS general substrate transporter"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50850","properties":[{"key":"EntryName","value":"MFS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSTEPLLSDSQRKTSLHSSPNASTYEAIPTRSSLSFELPEERRFSFGSEHEDNESNKISVEEETYYEEDRPWKYKMIALLCVLSLAVGSHYAAHTLGALKSVVKKELGISNSQYGVIQSSVSLVNTILPILGGVFIDTFGTSIGSILATSLIAIGNIFVALSTNLKSFVVMVIGRILYGIGSGTIITVQVAILSHWFKGKGLAIVVGIQIATSRMSSFLGNLTVVPIKEITGFYGWAFWFSAFLCVISLIINISYVLLMRILNERLSNQEMMNIKQKRHFSFKKLLLFPTIYWIFVLLEFQLGSAWTSFLHIHTELVKTRWNNTDEISDEYAAYNSSIAQFLPIFISPFLGYFLDRFGNRSLTLIMSTVFLTISMYLLGFIALTPIIVVIGMVCFSISLSLGPVGLLSSIPILLPLNYVGTALGIVKSSLNIGSTIYDILVGLLQDMDEDKYVMVMHLYLGSSVLSILVSILLYNVSKNWHNGILDMTEDERKENHDIIKIEESIQPTKRNYFYIIAFICTLIISWILFFIKFFND","length":537,"molWeight":60227,"crc64":"3FCB04674E68CF6E","md5":"869E0106DEEDB50E0C370885A3EFD1F7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":11,"Domain":1,"Region":1,"Compositional bias":2},"uniParcId":"UPI000EE46057"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397TIQ7","uniProtkbId":"A0A397TIQ7_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":29,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA97832.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361211"}],"value":"Histone acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361211"}],"value":"2.3.1.48"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA97832.1"}],"value":"C1645_751319"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045805"}],"value":"Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination. Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53908"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:13707"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:137954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53909"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24180"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:15921"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:131780"},{"database":"ChEBI","id":"CHEBI:144968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21992"},{"database":"Rhea","id":"RHEA-COMP:9845"},{"database":"Rhea","id":"RHEA-COMP:11338"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21993"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361211"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:45949"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361211"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010107"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361211"}],"value":"Belongs to the MYST (SAS/MOZ) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA97832.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":682,"modifier":"EXACT"}},"description":"MYST-type HAT","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51726"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":585,"modifier":"EXACT"},"end":{"value":585,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602717-51"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]},{"type":"Binding site","location":{"start":{"value":589,"modifier":"EXACT"},"end":{"value":589,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Modified residue","location":{"start":{"value":509,"modifier":"EXACT"},"end":{"value":509,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA97832.1"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022853"}],"id":"KW-0156","category":"Molecular function","name":"Chromatin regulator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361211"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA97832.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA97832.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000024","properties":[{"key":"ProteinId","value":"RIA97832.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397TIQ7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397TIQ7","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"787137at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:1990467","properties":[{"key":"GoTerm","value":"C:NuA3a histone acetyltransferase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003682","properties":[{"key":"GoTerm","value":"F:chromatin binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004402","properties":[{"key":"GoTerm","value":"F:histone acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003712","properties":[{"key":"GoTerm","value":"F:transcription coregulator activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0031507","properties":[{"key":"GoTerm","value":"P:heterochromatin formation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006357","properties":[{"key":"GoTerm","value":"P:regulation of transcription by RNA polymerase II"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"1.10.10.10:FF:000022","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.60.60:FF:000001","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.630.30:FF:000002","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.60.60","properties":[{"key":"EntryName","value":"N-acetyl transferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016181","properties":[{"key":"EntryName","value":"Acyl_CoA_acyltransferase"}]},{"database":"InterPro","id":"IPR002717","properties":[{"key":"EntryName","value":"HAT_MYST-type"}]},{"database":"InterPro","id":"IPR050603","properties":[{"key":"EntryName","value":"MYST_HAT"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR040706","properties":[{"key":"EntryName","value":"Zf-MYST"}]},{"database":"PANTHER","id":"PTHR10615","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10615:SF161","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE KAT7"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01853","properties":[{"key":"EntryName","value":"MOZ_SAS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17772","properties":[{"key":"EntryName","value":"zf-MYST"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55729","properties":[{"key":"EntryName","value":"Acyl-CoA N-acyltransferases (Nat)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51726","properties":[{"key":"EntryName","value":"MYST_HAT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEEKSIKNGIPSSSPTLPLQKEQISNPAVTSSKKTTTPRKRKANKLEEKMTEIKTETILTDQPVIKEEEQSITVIKEKRKRNRVLPQRGKKANNESPQLQTQQTTQLQNDITQEQTPPPPQQPEKSTSPIQISQKARSPSTQKRKAKTSAITGPIVKENSLDNSTPVIPLEEAGTSVFKEGPKEVVKEEQKEISEVRKSQKKTARIIIKQKRKRVIKSKETISSGDEDLEEESIPHNIIKTSSFNETSRMTLSSQTKSSKKRGITNGMDNNKELKARITRQRTKPTNKGKRGRKKLIKLEDEEVERNISKVSDTETIQNETEEKQDQASNHISENRLVENGEHGREQAEDVDLPFGGRLTADEADTSKTRPDYYDKVRFENAKNKAEAAMQPRQEITFDIEDQPQIFADATPKIRSIRFGDWEMDTWYVAPYPEEYSWYPTLYICEYCLKYMKSKYIADRHKMKCPMKHPPGDEIYRDGLISIFEVDGRKNTIYCQNLCLLAKMFLDHKTLYYDVEPFLFYVMTEINDTGCHFVGYFSKEKRSPLNYNVSCILTLPIHQRKGYGNLLIEFSYLLTKRESKTGSPEKPLSDLGLLSYRYYWRNVLFEVLNDSPEALSIEELSRKTSMTVNDVIATLQINNMLVRDENGIYRIVVDKDLIKNHLEKVTAKGYPRIRTENLRWTPFILTRVLRRAQDLENEKNMSTQEQQNSIDLFNKIVDKMDVDE","length":724,"molWeight":83655,"crc64":"35D64C1F399778CA","md5":"8A632886EDDE88648C779816B80747B8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":3,"Compositional bias":7,"Active site":1,"Binding site":1,"Modified residue":1},"uniParcId":"UPI000EC552A9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397TJG5","uniProtkbId":"A0A397TJG5_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA98363.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfate adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"2.7.7.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"ATP-sulfurylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfate adenylate transferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"SAT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"MET3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA98363.1"}],"value":"C1645_870734"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24152"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58243"},{"database":"ChEBI","id":"CHEBI:58339"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001823"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sulfate + ATP + H(+) = adenosine 5'-phosphosulfate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18133"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16189"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58243"}],"ecNumber":"2.7.7.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Homohexamer. Dimer of trimers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"In the C-terminal section; belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"In the N-terminal section; belongs to the sulfate adenylyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA98363.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"ATP-sulfurylase PUA-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14306"}]},{"type":"Domain","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Sulphate adenylyltransferase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01747"}]},{"type":"Domain","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":548,"modifier":"EXACT"}},"description":"APS kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01583"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"N-terminal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Region","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":574,"modifier":"EXACT"}},"description":"Allosteric regulation domain; adenylyl-sulfate kinase-like","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58339"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"3'-phosphoadenylyl sulfate","id":"ChEBI:CHEBI:58339","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":516,"modifier":"EXACT"},"end":{"value":516,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58339"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"3'-phosphoadenylyl sulfate","id":"ChEBI:CHEBI:58339","note":"allosteric inhibitor"}},{"type":"Site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Site","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Induces change in substrate recognition on ATP binding","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0198","category":"Biological process","name":"Cysteine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA98363.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA98363.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000016","properties":[{"key":"ProteinId","value":"RIA98363.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397TJG5","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397TJG5","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"468at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00097","properties":[{"key":"RectionId","value":"-"}]},{"database":"UniPathway","id":"UPA00140","properties":[{"key":"RectionId","value":"UER00204"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004020","properties":[{"key":"GoTerm","value":"F:adenylylsulfate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004781","properties":[{"key":"GoTerm","value":"F:sulfate adenylyltransferase (ATP) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070814","properties":[{"key":"GoTerm","value":"P:hydrogen sulfide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000103","properties":[{"key":"GoTerm","value":"P:sulfate assimilation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02027","properties":[{"key":"EntryName","value":"APSK"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00517","properties":[{"key":"EntryName","value":"ATPS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.400.10:FF:000003","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000802","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000052","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.400.10","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03106","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002891","properties":[{"key":"EntryName","value":"APS"}]},{"database":"InterPro","id":"IPR059117","properties":[{"key":"EntryName","value":"APS_kinase_dom"}]},{"database":"InterPro","id":"IPR025980","properties":[{"key":"EntryName","value":"ATP-Sase_PUA-like_dom"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR015947","properties":[{"key":"EntryName","value":"PUA-like_sf"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"InterPro","id":"IPR027535","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_euk"}]},{"database":"InterPro","id":"IPR050512","properties":[{"key":"EntryName","value":"Sulf_AdTrans/APS_kinase"}]},{"database":"InterPro","id":"IPR024951","properties":[{"key":"EntryName","value":"Sulfurylase_cat_dom"}]},{"database":"InterPro","id":"IPR002650","properties":[{"key":"EntryName","value":"Sulphate_adenylyltransferase"}]},{"database":"NCBIfam","id":"TIGR00455","properties":[{"key":"EntryName","value":"apsK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004040","properties":[{"key":"EntryName","value":"PRK05537.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00339","properties":[{"key":"EntryName","value":"sopT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42700","properties":[{"key":"EntryName","value":"SULFATE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42700:SF1","properties":[{"key":"EntryName","value":"SULFATE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01583","properties":[{"key":"EntryName","value":"APS_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01747","properties":[{"key":"EntryName","value":"ATP-sulfurylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14306","properties":[{"key":"EntryName","value":"PUA_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88697","properties":[{"key":"EntryName","value":"PUA domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MANSPHGGVLKDLHARDASKKEQLFAEVEKLPSIVLSDRQLCDLELIMNGGFSPLEGFMNQEDYQSVVKDLRLKNGLLFSMPITLDVSDQDIKTLELEPKKRIVLRDPRDDAPLAILTIQDIYKPDKVEEAIKVFGDNDIAHPGVKYLHNQTKEFYVGGSVEAIQNLIHYDYIAHRHTPAELRAHFKKLHWTRVVAFQTRNPMHRAHRELTVRAARNRQANVLIHPVVGLTKPGDIDHYTRVRVYQALMPKYPNGMAALSLLPLAMRMGGPREAVWHAIIRKNFGNTHFIVGRDHAGPGKNSRGVDFYGPYDAQKLVAKYKDELDIEVVPFQMVTYIPDSDEYLPVDEIPEGTTTLNISGTELRRRLRTGGHIPEWFSYPEVVKVLRETHPPKSKQGFTLFLTGYYNSGKKAIGKALQVVLNEQGGRSVTLLLGETVRHGISSELGFSKKDRDQNIARIAFVSAELTKAGAAVIAAPIAPFAEARAQAKTHIETYGAFYLIHVNTPLDYCIKTDRKGIYKKAQSGEIKNFTGVDDPYEAPTDADIVVDASKQCISEICHQIVLLLEKDGYIGER","length":574,"molWeight":64402,"crc64":"85790686989B9D15","md5":"B9B604833D5A0934B8134B9506790B05"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":2,"Active site":3,"Binding site":8,"Site":3},"uniParcId":"UPI000ED519BB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397S3F3","uniProtkbId":"A0A397S3F3_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80940.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012527"}],"value":"diphosphoinositol-polyphosphate diphosphatase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012527"}],"value":"3.6.1.52"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80940.1"}],"value":"C1645_582166"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate + H2O = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79699"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:74946"},{"database":"ChEBI","id":"CHEBI:77983"}],"ecNumber":"3.6.1.52","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047927"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:79700"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047927"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3,5-bis(diphospho)-1D-myo-inositol 1,2,4,6-tetrakisphosphate + H2O = 3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:56312"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:140372"},{"database":"ChEBI","id":"CHEBI:140374"}],"ecNumber":"3.6.1.52","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047562"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:56313"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047562"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + H2O = 1D-myo-inositol hexakisphosphate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22384"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58130"},{"database":"ChEBI","id":"CHEBI:58628"}],"ecNumber":"3.6.1.52","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047342"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:22385"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047342"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"6-diphospho-1D-myo-inositol pentakisphosphate + H2O = 1D-myo-inositol hexakisphosphate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79703"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58130"},{"database":"ChEBI","id":"CHEBI:230534"}],"ecNumber":"3.6.1.52","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048424"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:79704"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048424"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10684"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20101"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:61978"}],"ecNumber":"3.1.3.48","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10044"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044949"}],"value":"Belongs to the protein-tyrosine phosphatase family. Atypical dual-specificity phosphatase Siw14-like subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80940.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"Tyrosine-protein phosphatase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50054"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"Phosphocysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00160"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00160"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00160"}],"id":"KW-0904","category":"Molecular function","name":"Protein phosphatase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80940.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80940.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000874","properties":[{"key":"ProteinId","value":"RIA80940.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397S3F3","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397S3F3","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"6375174at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0052840","properties":[{"key":"GoTerm","value":"F:inositol diphosphate tetrakisphosphate diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004725","properties":[{"key":"GoTerm","value":"F:protein tyrosine phosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008138","properties":[{"key":"GoTerm","value":"F:protein tyrosine/serine/threonine phosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd14528","properties":[{"key":"EntryName","value":"PFA-DSP_Siw14"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.190.10:FF:000024","properties":[{"key":"EntryName","value":"probable tyrosine-protein phosphatase At1g05000"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.190.10","properties":[{"key":"EntryName","value":"Protein tyrosine phosphatase superfamily"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR020428","properties":[{"key":"EntryName","value":"PFA-DSPs"}]},{"database":"InterPro","id":"IPR029021","properties":[{"key":"EntryName","value":"Prot-tyrosine_phosphatase-like"}]},{"database":"InterPro","id":"IPR004861","properties":[{"key":"EntryName","value":"Siw14-like"}]},{"database":"InterPro","id":"IPR016130","properties":[{"key":"EntryName","value":"Tyr_Pase_AS"}]},{"database":"InterPro","id":"IPR020422","properties":[{"key":"EntryName","value":"TYR_PHOSPHATASE_DUAL_dom"}]},{"database":"PANTHER","id":"PTHR31126:SF48","properties":[{"key":"EntryName","value":"INOSITOL PHOSPHATASE SIW14"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31126","properties":[{"key":"EntryName","value":"TYROSINE-PROTEIN PHOSPHATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03162","properties":[{"key":"EntryName","value":"Y_phosphatase2"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01911","properties":[{"key":"EntryName","value":"PFDSPHPHTASE"}]},{"database":"SUPFAM","id":"SSF52799","properties":[{"key":"EntryName","value":"(Phosphotyrosine protein) phosphatases II"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00383","properties":[{"key":"EntryName","value":"TYR_PHOSPHATASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50054","properties":[{"key":"EntryName","value":"TYR_PHOSPHATASE_DUAL"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTKEAKEAKEEDSSSSISNTATTVTTFTSTLSFQRTQSWSTASSSGEEQQKFEEELIPPDNFNMVSNWVYRSSFPKKKNFAFLKKLGLKSILTLILEEYPEQNMKFLKANDIKFFQFEIAGNKEPFCHIPEDKICAALAVILDRRNHPILIHCNKGKHRTGCLIGCLRKLQRWTYTSIFDEYRRFSHPKSRSMDQQFIELFDVSQVWKLIDRNYVPNWDVLGCPW","length":226,"molWeight":26353,"crc64":"BF3614B2CCC5F887","md5":"54CDB76FFD1D1BDBC900C51B44252561"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":5,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":2,"Active site":1},"uniParcId":"UPI000EC65D27"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397S5K1","uniProtkbId":"A0A397S5K1_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80772.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00078532"}],"value":"Glutamic--alanine transaminase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00026106"}],"value":"2.6.1.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066546"}],"value":"2.6.1.4"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013049"}],"value":"2.6.1.44"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00080525"}],"value":"Glutamic--pyruvic transaminase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80772.1"}],"value":"C1645_838086"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanine + 2-oxoglutarate = pyruvate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19453"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57972"}],"ecNumber":"2.6.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047412"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycine + 2-oxoglutarate = glyoxylate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14089"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:36655"},{"database":"ChEBI","id":"CHEBI:57305"}],"ecNumber":"2.6.1.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glyoxylate + L-alanine = glycine + pyruvate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24248"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:36655"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:57972"}],"ecNumber":"2.6.1.44","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001781"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025708"}],"value":"Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004275"}],"value":"Peroxisome","id":"SL-0204"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025785"}],"value":"Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80772.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"Aminotransferase class I/classII large","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00155"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022576"}],"id":"KW-0032","category":"Molecular function","name":"Aminotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023140"}],"id":"KW-0576","category":"Cellular component","name":"Peroxisome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80772.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80772.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80772.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000899","properties":[{"key":"ProteinId","value":"RIA80772.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397S5K1","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397S5K1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"1732682at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00528","properties":[{"key":"RectionId","value":"UER00586"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008483","properties":[{"key":"GoTerm","value":"F:transaminase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042853","properties":[{"key":"GoTerm","value":"P:L-alanine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd00609","properties":[{"key":"EntryName","value":"AAT_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.287.1970:FF:000001","properties":[{"key":"EntryName","value":"Alanine aminotransferase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000012","properties":[{"key":"EntryName","value":"alanine aminotransferase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.1150.10:FF:000010","properties":[{"key":"EntryName","value":"Alanine aminotransferase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.287.1970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045088","properties":[{"key":"EntryName","value":"ALAT1/2-like"}]},{"database":"InterPro","id":"IPR004839","properties":[{"key":"EntryName","value":"Aminotransferase_I/II_large"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"PANTHER","id":"PTHR11751","properties":[{"key":"EntryName","value":"ALANINE AMINOTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11751:SF29","properties":[{"key":"EntryName","value":"ALANINE TRANSAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00155","properties":[{"key":"EntryName","value":"Aminotran_1_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSQRALPAKILTYESINPHVKRVEYAVRGELAIRAEKLKDELSKGNSHNYNFDTVVNCNIGNPQQLKQKPITFFRQVASLMEYPDLLLPENRTQVEALYPIDAIERAQKLLEQIGSVGAYSHSQGIPYIRNHVAKFIEERDGYPANPNDIFLTQGASAGVQNILQLIITHSNVGIMIPIPQYPLYTATLALYDAQPVPYYLNEEEDWGLDISQLTSSLSAGRSKGLDTRALVIINPGNPTGQCLTEQNMREIINFCHNERIILLADEVYQTNIYQPAERPFHSFKKVLRSMGRKYEQFELFSFHSVSKGMIGECGRRGGYYECTNIDSRVVEELYKIASVSLCPNVQGQIMVDLMVQPPKRSDESYTLYQKEVDEIYMSLRRRSTKLSECFNQLEGVTCNSAQGSMYLFPRIRLPQKAIEAAHQAGKQPDEFYCLAMLDATGVCVVPGSGFGQKNGTLHFRSTFLPPEELFDGFCTRLQRFHNEFLERYHD","length":491,"molWeight":55797,"crc64":"91891893F46E8BEB","md5":"197FA7482966245D05FDF3617F620A4A"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI000EC42BC7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397S673","uniProtkbId":"A0A397S673_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":26,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80249.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"value":"Lipoyl synthase, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"value":"2.8.1.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"value":"Lipoate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"value":"LS"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"value":"Lip-syn"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"value":"Lipoic acid synthase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80249.1"}],"value":"C1645_800389"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"value":"Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine + 4 H(+) = [[Fe-S] cluster scaffold protein] + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 5'-deoxyadenosine + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16585"},{"database":"Rhea","id":"RHEA-COMP:9928"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10475"},{"database":"Rhea","id":"RHEA-COMP:14568"},{"database":"Rhea","id":"RHEA-COMP:14569"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:29034"},{"database":"ChEBI","id":"CHEBI:29919"},{"database":"ChEBI","id":"CHEBI:33722"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:78809"},{"database":"ChEBI","id":"CHEBI:83100"}],"ecNumber":"2.8.1.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047326"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"value":"Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"value":"Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004173"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"value":"Belongs to the radical SAM superfamily. Lipoyl synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80249.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Binding site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03123"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80249.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80249.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01001012","properties":[{"key":"ProteinId","value":"RIA80249.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397S673","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397S673","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"3231at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00538","properties":[{"key":"RectionId","value":"UER00593"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016992","properties":[{"key":"GoTerm","value":"F:lipoate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009249","properties":[{"key":"GoTerm","value":"P:protein lipoylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000036","properties":[{"key":"EntryName","value":"Lipoyl synthase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00206","properties":[{"key":"EntryName","value":"Lipoyl_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR006638","properties":[{"key":"EntryName","value":"Elp3/MiaA/NifB-like_rSAM"}]},{"database":"InterPro","id":"IPR031691","properties":[{"key":"EntryName","value":"LIAS_N"}]},{"database":"InterPro","id":"IPR003698","properties":[{"key":"EntryName","value":"Lipoyl_synth"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00510","properties":[{"key":"EntryName","value":"lipA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004019","properties":[{"key":"EntryName","value":"PRK05481.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009544","properties":[{"key":"EntryName","value":"PRK12928.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10949","properties":[{"key":"EntryName","value":"LIPOYL SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10949:SF0","properties":[{"key":"EntryName","value":"LIPOYL SYNTHASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16881","properties":[{"key":"EntryName","value":"LIAS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005963","properties":[{"key":"EntryName","value":"Lipoyl_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00271","properties":[{"key":"EntryName","value":"lipoyl_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01058","properties":[{"key":"EntryName","value":"lipoyl_synthase_like"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00729","properties":[{"key":"EntryName","value":"Elp3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNSMQVQNAFFFVKAFGYILRISRFSEKLASGPSLDDFIIANSKIEKLNLDLQNTLVTNEKSKKIPYRRLPEWLKTKVPVGANFARIKRDLRGLNLHTVCEEARCPNIGDCWGGGEHKTATATIMLMGDECTRGCRFCSVKTSRTPKPLDQNEPENVANAISKWGLDYIVLTSVDRDDLSDGGSEHFAKTVRLLKKKAPHILVECLTGDFQGNLDCVTKLATSGLDVYAHNIETVESLTSCIRDRRATFRQSLNVLEHAKKIKPSLITKTSIMLGVGETDEEVLDAMKELRKVNVDCVTLGQYMRPTKRNMKVQEYIAPEKFDYWAKIGNDLGFLYTASGPLVRSSYKAGEFYIGNILRKKII","length":363,"molWeight":40841,"crc64":"4B3E144472E839D4","md5":"49DC6313F2489334AB599BA2D34CA84A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":10},"uniParcId":"UPI000EB8BF38"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397S6K7","uniProtkbId":"A0A397S6K7_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA82013.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"E3 ubiquitin-protein ligase PEP5"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"2.3.2.27"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA82013.1"}],"value":"C1645_881286"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.","ecNumber":"2.3.2.27","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"Component of the homotypic vacuole fusion and vacuole protein sorting (HOPS) complex. Component of the class C core vacuole/endosome tethering (CORVET) complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029433"}],"value":"Endomembrane system","id":"SL-0147"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029433"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029433"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"Vacuole membrane","id":"SL-0271"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007070"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"Belongs to the VPS11 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA82013.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Repeat","location":{"start":{"value":418,"modifier":"EXACT"},"end":{"value":566,"modifier":"EXACT"}},"description":"CHCR","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01006"}]},{"type":"Domain","location":{"start":{"value":959,"modifier":"EXACT"},"end":{"value":994,"modifier":"EXACT"}},"description":"RING-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50089"}]},{"type":"Region","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":920,"modifier":"EXACT"},"end":{"value":950,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Compositional bias","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022927"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0653","category":"Biological process","name":"Protein transport"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0813","category":"Biological process","name":"Transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0833","category":"Biological process","name":"Ubl conjugation pathway"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0926","category":"Cellular component","name":"Vacuole"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00175"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA82013.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA82013.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000714","properties":[{"key":"ProteinId","value":"RIA82013.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397S6K7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397S6K7","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"26184at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0033263","properties":[{"key":"GoTerm","value":"C:CORVET complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000329","properties":[{"key":"GoTerm","value":"C:fungal-type vacuole membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030897","properties":[{"key":"GoTerm","value":"C:HOPS complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030674","properties":[{"key":"GoTerm","value":"F:protein-macromolecule adaptor activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061630","properties":[{"key":"GoTerm","value":"F:ubiquitin protein ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0007032","properties":[{"key":"GoTerm","value":"P:endosome organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006886","properties":[{"key":"GoTerm","value":"P:intracellular protein transport"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048284","properties":[{"key":"GoTerm","value":"P:organelle fusion"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0007033","properties":[{"key":"GoTerm","value":"P:vacuole organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016192","properties":[{"key":"GoTerm","value":"P:vesicle-mediated transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd16688","properties":[{"key":"EntryName","value":"RING-H2_Vps11"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.25.40.10","properties":[{"key":"EntryName","value":"Tetratricopeptide repeat domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.130.10.10","properties":[{"key":"EntryName","value":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016024","properties":[{"key":"EntryName","value":"ARM-type_fold"}]},{"database":"InterPro","id":"IPR057308","properties":[{"key":"EntryName","value":"CHCR_PEP5_VPS11"}]},{"database":"InterPro","id":"IPR000547","properties":[{"key":"EntryName","value":"Clathrin_H-chain/VPS_repeat"}]},{"database":"InterPro","id":"IPR057307","properties":[{"key":"EntryName","value":"PEP5_VPS11_N"}]},{"database":"InterPro","id":"IPR011990","properties":[{"key":"EntryName","value":"TPR-like_helical_dom_sf"}]},{"database":"InterPro","id":"IPR016528","properties":[{"key":"EntryName","value":"VPS11"}]},{"database":"InterPro","id":"IPR024763","properties":[{"key":"EntryName","value":"VPS11_C"}]},{"database":"InterPro","id":"IPR015943","properties":[{"key":"EntryName","value":"WD40/YVTN_repeat-like_dom_sf"}]},{"database":"InterPro","id":"IPR036322","properties":[{"key":"EntryName","value":"WD40_repeat_dom_sf"}]},{"database":"InterPro","id":"IPR001841","properties":[{"key":"EntryName","value":"Znf_RING"}]},{"database":"PANTHER","id":"PTHR23323","properties":[{"key":"EntryName","value":"VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23323:SF24","properties":[{"key":"EntryName","value":"VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF23341","properties":[{"key":"EntryName","value":"PEP5_VPS11_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF23356","properties":[{"key":"EntryName","value":"TPR_PEP5_VPS11"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF12451","properties":[{"key":"EntryName","value":"VPS11_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF007860","properties":[{"key":"EntryName","value":"VPS11"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48371","properties":[{"key":"EntryName","value":"ARM repeat"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF57850","properties":[{"key":"EntryName","value":"RING/U-box"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50978","properties":[{"key":"EntryName","value":"WD40 repeat-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50236","properties":[{"key":"EntryName","value":"CHCR"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50089","properties":[{"key":"EntryName","value":"ZF_RING_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MHHVKLESRTVLIFLNIMSVKQWRQFNFFDVQQIKDPHDSTKTPAIFQKTDITVSTSGRGNIILADSSGYVHIVDRSFNVQSFIAYEGGRVTHMKQIKQKNILLTVGEEDFPIIKIWDLDKQDKSKGIPTCLRTIKVNHGGKPFPVSTLAVLDNLAQIAVGLANGVVVLIRGDLRDRHTKQKVIHESDEPVTGLGFKENSKTIILFIVTTNKVLTCITTSRNVPMVIDDQGCALGCAVISDTIHEMVVAKDEGIYFYGPEGRGACFAYEGTKSSVTWFKSNLIIVSPPAPQSTRHTTTSRTDSPLQNNNSPFELTKVTIFDTANKFIAYMGTFSHGVRTICCEWGGIYILGMDGKLYRLEEKDTPTKLEILFKKNLYLLAINLAHSQKYDDANISEIFKKYGDHLYSKADYDGAMAQYIRTIGQLEPSYIIRKFLDAQRIHNLVNYLQELHSHDLANPDHTTLLLNCYTKLKDVARLDQFIKTDSKLNFDLETAIKVCRQAGYYEHAVYLAKLGEEHDLYLKIQIEDVEDYENALEYIRNLGSFEADRNLQKYGKILLNHLPEPTTKLLIDLCTGDLYLAAQRARTPEPIVPTEQSHPGGIPYASFLQFAHAQSSNASNTSNASNLEVQTNVTAVNIRQTKEPKTVAYKPPPVRTFMSLFVDQPNYLIQFLEQVSQKRWGSFGSVKPSQPAHNLSLAKGHYVPADNDADKRAESLKSFVEPDTETEEKKAVWNTLLELYLSEAYLPPVISTKDAKGRKFGAPGIFGVATETERVTEKLIRKDKALQLLKDENISYDANQALVLCYLAHFDEGIIYLYEKMTMYEDILRFYMAKDNTEKVIEALKKYGSQDQSLYPLTLTYFSSSPATLETSTTELLKILDHIDSHNLLPPLQVVQALSRNSVATLGMVKSYLGKRIELEKKEAQADMKLIQSYREETEKKRKEIDDLKTVARIFQVTKCTGCRGTLDLPAIHFLCRHSFHQRCLPDNDRECPQCAIQHRMISEIRRAQEENAEKHELFFEQLKEADDGFSVIADYFSKNTMAFAKLID","length":1048,"molWeight":118773,"crc64":"CED31DEDAF6CB738","md5":"A7F515A48C1C91A5726E9698B7DD3A01"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Repeat":1,"Domain":1,"Region":1,"Coiled coil":1,"Compositional bias":1},"uniParcId":"UPI000ED27A7D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397S6Q0","uniProtkbId":"A0A397S6Q0_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-12-05","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80429.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012119"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"Adenosine kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"AK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012119"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"2.7.1.20"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"Adenosine 5'-phosphotransferase"}}],"flag":"Fragment"},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80429.1"}],"value":"C1645_792574"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine + ATP = AMP + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20824"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16335"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.20","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010688"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"value":"Belongs to the carbohydrate kinase PfkB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80429.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"Carbohydrate kinase PfkB","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00294"}]},{"type":"Active site","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR601805-1"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80429.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022726"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0660","category":"Biological process","name":"Purine salvage"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368116"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80429.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80429.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000971","properties":[{"key":"ProteinId","value":"RIA80429.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397S6Q0","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397S6Q0","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"432447at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00588","properties":[{"key":"RectionId","value":"UER00659"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004001","properties":[{"key":"GoTerm","value":"F:adenosine kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044209","properties":[{"key":"GoTerm","value":"P:AMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006144","properties":[{"key":"GoTerm","value":"P:purine nucleobase metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006166","properties":[{"key":"GoTerm","value":"P:purine ribonucleoside salvage"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01168","properties":[{"key":"EntryName","value":"adenosine_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1110.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001805","properties":[{"key":"EntryName","value":"Adenokinase"}]},{"database":"InterPro","id":"IPR002173","properties":[{"key":"EntryName","value":"Carboh/pur_kinase_PfkB_CS"}]},{"database":"InterPro","id":"IPR011611","properties":[{"key":"EntryName","value":"PfkB_dom"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"PANTHER","id":"PTHR45769","properties":[{"key":"EntryName","value":"ADENOSINE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45769:SF3","properties":[{"key":"EntryName","value":"ADENOSINE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00294","properties":[{"key":"EntryName","value":"PfkB"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00989","properties":[{"key":"EntryName","value":"ADENOKINASE"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00584","properties":[{"key":"EntryName","value":"PFKB_KINASES_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"YNSEKVEKLIEKYGLSPKSTNEDLNKFNEFLNEVSKYPDTLKVSGGTAQNSLRGAQRLLPSNSTVFIGYIGKDENGKTLKKTLNNDGVRTEYTELDDYPTGVVSYSKLSNNKYFIKYNRGAATQFKLADIKSPSKWKLIENAKYFYVCKTNFDIVQEISKHALENDKIFATNLSSINYVTKFKHQIDEISPYWDIVFGNESEALAFAKMSNWNTEDIFEVAKKIAQLPKFSTNFIRMTVITRDKESTIYSNQKGVVKEYPIIPVDENDLVDVTGAGDSFVGGFLSRLIQGKNIDECIMTGHKLANYIVKQVGTQYGSFNE","length":320,"molWeight":36258,"crc64":"20170720CB98A8FA","md5":"F85790CAE53A8FE55E5C29D31DF19207"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Non-terminal residue":1},"uniParcId":"UPI000EDB4D10"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397S6R6","uniProtkbId":"A0A397S6R6_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":35,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81678.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368061"}],"value":"DNA replication licensing factor MCM3"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368061"}],"value":"3.6.4.12"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81678.1"}],"value":"C1645_836595"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368061"}],"value":"Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"3.6.4.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047995"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368061"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368061"}],"value":"Component of the MCM2-7 complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368061"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008010"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004070"}],"value":"Belongs to the MCM family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81678.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":676,"modifier":"EXACT"}},"description":"MCM C-terminal AAA(+) ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50051"}]},{"type":"Region","location":{"start":{"value":679,"modifier":"EXACT"},"end":{"value":758,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":364,"modifier":"EXACT"}},"description":"Walker A","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}]},{"type":"Motif","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":424,"modifier":"EXACT"}},"description":"Walker B","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}]},{"type":"Compositional bias","location":{"start":{"value":689,"modifier":"EXACT"},"end":{"value":708,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":719,"modifier":"EXACT"},"end":{"value":728,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":742,"modifier":"EXACT"},"end":{"value":758,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Site","location":{"start":{"value":490,"modifier":"EXACT"},"end":{"value":490,"modifier":"EXACT"}},"description":"Arginine finger","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022705"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368061"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368061"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01410"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81678.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81678.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000759","properties":[{"key":"ProteinId","value":"RIA81678.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397S6R6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397S6R6","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"1882346at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0000785","properties":[{"key":"GoTerm","value":"C:chromatin"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0031261","properties":[{"key":"GoTerm","value":"C:DNA replication preinitiation complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0042555","properties":[{"key":"GoTerm","value":"C:MCM complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005656","properties":[{"key":"GoTerm","value":"C:nuclear pre-replicative complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0043596","properties":[{"key":"GoTerm","value":"C:nuclear replication fork"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0003697","properties":[{"key":"GoTerm","value":"F:single-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0017116","properties":[{"key":"GoTerm","value":"F:single-stranded DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006271","properties":[{"key":"GoTerm","value":"P:DNA strand elongation involved in DNA replication"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000727","properties":[{"key":"GoTerm","value":"P:double-strand break repair via break-induced replication"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:1902975","properties":[{"key":"GoTerm","value":"P:mitotic DNA replication initiation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006279","properties":[{"key":"GoTerm","value":"P:premeiotic DNA replication"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"FunFam","id":"2.20.28.10:FF:000008","properties":[{"key":"EntryName","value":"DNA helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.20.28.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1640.10","properties":[{"key":"EntryName","value":"mini-chromosome maintenance (MCM) complex, chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.140","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR031327","properties":[{"key":"EntryName","value":"MCM"}]},{"database":"InterPro","id":"IPR008046","properties":[{"key":"EntryName","value":"Mcm3"}]},{"database":"InterPro","id":"IPR018525","properties":[{"key":"EntryName","value":"MCM_CS"}]},{"database":"InterPro","id":"IPR001208","properties":[{"key":"EntryName","value":"MCM_dom"}]},{"database":"InterPro","id":"IPR041562","properties":[{"key":"EntryName","value":"MCM_lid"}]},{"database":"InterPro","id":"IPR027925","properties":[{"key":"EntryName","value":"MCM_N"}]},{"database":"InterPro","id":"IPR033762","properties":[{"key":"EntryName","value":"MCM_OB"}]},{"database":"InterPro","id":"IPR012340","properties":[{"key":"EntryName","value":"NA-bd_OB-fold"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR056575","properties":[{"key":"EntryName","value":"WH_MCM3_C"}]},{"database":"PANTHER","id":"PTHR11630","properties":[{"key":"EntryName","value":"DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11630:SF46","properties":[{"key":"EntryName","value":"DNA REPLICATION LICENSING FACTOR MCM3-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00493","properties":[{"key":"EntryName","value":"MCM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17855","properties":[{"key":"EntryName","value":"MCM_lid"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14551","properties":[{"key":"EntryName","value":"MCM_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17207","properties":[{"key":"EntryName","value":"MCM_OB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF23191","properties":[{"key":"EntryName","value":"WHD_MCM3_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01657","properties":[{"key":"EntryName","value":"MCMFAMILY"}]},{"database":"PRINTS","id":"PR01659","properties":[{"key":"EntryName","value":"MCMPROTEIN3"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00350","properties":[{"key":"EntryName","value":"MCM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50249","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00847","properties":[{"key":"EntryName","value":"MCM_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50051","properties":[{"key":"EntryName","value":"MCM_CTD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MASNTDLQKLQDEAFLDRVRFFEEFLEADKERLGIEKFYKVEIVQMLRKGERRFIVNLNELRYYHAENAKKLEESPNEWIPAFEKALKNIIKNISSDIGDEINTNIEEQNFYIGFNGTFHHHVNPRTLKSIHLGKLICIEGIVSRCSLVRLKLAKSVHYCEKTGNFCSKEYHDSTSIGSQIPSSSAYPTEDENGNPLTTEFGYSVYRDHQTICLQEMPEKMPPGLLTRSIDIILDDDLVDKVKPGDRIQLAGCYRAIGKPSQGSTSATFKTVIIANNVTILSGEIGLKVITDIDIANIEKISKNENIFELLSRSLAPSIYGHDMVKKAILLMLLGGKEQNLSSGTHIRGDINILMVGDPSTSKSQLLRRVLNIAPLAIATTGRGSTGVGLTAAVTRDKETGEKSLEAGAMVLGDRGVVCIDEFDKMIDTDRVAIHEVMEQQTVTIAKAGIHTSLNARCSVIAAANPIYGQYNIHKDPAHNIALPDSLLSRFDLVFVITDEINEVRDSLISRHVLRLHEYRPPNLEEGVPIKEDSGQTIFMEEAEKNTEPTPVYMQYDLLLNDNNDDQRDPDTNSDQTNFLSSEFLKKYIQYAKSHEEPRLGKAAAAYLCELWVNLRNEKETDGQAKTSPLTPRALDSLFRLATAHTKARLGKRVTIKDAKVAEEIVRFALFKEVSIKDRRKRRKTNVNENDELDSDDDNDDTNDDSDKDENSSQRSINTRKDKGKGKMIESPTDDTQQFDSSSKETEDNMDTDETRKQSFAELNFDTLIIEDSIEIITSDRLRLFQENLNRITSSPPYENSISLESLIREINNNLPENQAYTSEEVNAALKKMQDRNKVMISDDTVYII","length":849,"molWeight":95776,"crc64":"2FC4420F9E28ACF5","md5":"C903D95F2F390B0639CD984C45B4CC43"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Motif":2,"Compositional bias":3,"Site":1},"uniParcId":"UPI000ECD406F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397S8M7","uniProtkbId":"A0A397S8M7_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":20,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80357.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00068357"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"value":"RNA cytidine acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"value":"2.3.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"value":"18S rRNA cytosine acetyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"value":"NAT10"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80357.1"}],"value":"C1645_792689"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"value":"RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tRNAs. Requires the tRNA-binding adapter protein TAN1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a cytidine in 18S rRNA + acetyl-CoA + ATP + H2O = an N(4)-acetylcytidine in 18S rRNA + ADP + phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:51424"},{"database":"Rhea","id":"RHEA-COMP:13575"},{"database":"Rhea","id":"RHEA-COMP:13576"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:74900"},{"database":"ChEBI","id":"CHEBI:82748"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052133"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a cytidine in tRNA + acetyl-CoA + ATP + H2O = an N(4)-acetylcytidine in tRNA + ADP + phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53876"},{"database":"Rhea","id":"RHEA-COMP:13670"},{"database":"Rhea","id":"RHEA-COMP:13671"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:74900"},{"database":"ChEBI","id":"CHEBI:82748"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"value":"Interacts with TAN1"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004604"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"value":"Nucleus, nucleolus","id":"SL-0188"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"value":"Belongs to the RNA cytidine acetyltransferase family. NAT10 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80357.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"TmcA/NAT10 N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08351"}]},{"type":"Domain","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"TcmA/NAT10 helicase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF05127"}]},{"type":"Domain","location":{"start":{"value":545,"modifier":"EXACT"},"end":{"value":775,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13718"}]},{"type":"Domain","location":{"start":{"value":787,"modifier":"EXACT"},"end":{"value":1035,"modifier":"EXACT"}},"description":"Possible tRNA binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13725"}]},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":487,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":646,"modifier":"EXACT"},"end":{"value":648,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":653,"modifier":"EXACT"},"end":{"value":659,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":747,"modifier":"EXACT"},"end":{"value":747,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"id":"KW-0698","category":"Biological process","name":"rRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03211"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80357.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA80357.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000986","properties":[{"key":"ProteinId","value":"RIA80357.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397S8M7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397S8M7","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"10067491at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0030686","properties":[{"key":"GoTerm","value":"C:90S preribosome"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005730","properties":[{"key":"GoTerm","value":"C:nucleolus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:1990883","properties":[{"key":"GoTerm","value":"F:18S rRNA cytidine N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0051392","properties":[{"key":"GoTerm","value":"F:tRNA cytidine N4-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:1904812","properties":[{"key":"GoTerm","value":"P:rRNA acetylation involved in maturation of SSU-rRNA"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051391","properties":[{"key":"GoTerm","value":"P:tRNA acetylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.50.11040:FF:000002","properties":[{"key":"EntryName","value":"RNA cytidine acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:002218","properties":[{"key":"EntryName","value":"tRNA(Met) cytidine acetyltransferase TmcA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.11040","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03211","properties":[{"key":"EntryName","value":"RNA_acetyltr_Nat10"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000182","properties":[{"key":"EntryName","value":"GNAT_dom"}]},{"database":"InterPro","id":"IPR033688","properties":[{"key":"EntryName","value":"NAT10"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR007807","properties":[{"key":"EntryName","value":"TcmA/NAT10_helicase"}]},{"database":"InterPro","id":"IPR032672","properties":[{"key":"EntryName","value":"TmcA/NAT10/Kre33"}]},{"database":"InterPro","id":"IPR013562","properties":[{"key":"EntryName","value":"TmcA/NAT10_N"}]},{"database":"InterPro","id":"IPR027992","properties":[{"key":"EntryName","value":"tRNA_bind_dom"}]},{"database":"PANTHER","id":"PTHR10925","properties":[{"key":"EntryName","value":"N-ACETYLTRANSFERASE 10"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10925:SF5","properties":[{"key":"EntryName","value":"RNA CYTIDINE ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13718","properties":[{"key":"EntryName","value":"GNAT_acetyltr_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05127","properties":[{"key":"EntryName","value":"NAT10_TcmA_helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08351","properties":[{"key":"EntryName","value":"TmcA_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13725","properties":[{"key":"EntryName","value":"tRNA_bind_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVKKVIDSRINTLVKNGVQNQHRTFFIIVGDKGKEQVVNLHWLLSQAQVSARPSVLWCYKKELGFSSHRKKREAKIKKEIKRGIREPNTEDPFELFVAVTNIRYTYYKETHKILGNTYGMCVLQDFEALTPNLLARTIETIEGGGIIIILLKTMKSLKQLYTLTMDVHSRYRTEAHDDVTARFNERFILSLGSCENCLVVDDELNVLPISTGKNVKPLSLKNPEHLLTEQQVELKELKASLADTQPVGSLVATAKTLDQAKAILTFIESISEKTLRSTVALTASRGRGKSAALGIAIASAVAYGYSNIFVTSPSPENLKTLFEFIFKGFDALHYEEHLDYDIVQSTNPDFNGAIVRVNIFRQHRQTIQYIQPQDAHVLGQAELVVIDEAAAIPLPLVKSLIGPYLVFMASTINGYEGTGRSLSLKLIQQLREKSKGFIGKEGRTDVSDDIVIVGRGRKADKEVSSTLNGATAGGRVLREIKLEEPIRYALNDPVEKWLNKLLCLDASIVPKNIQGCPHPQKCELYYVNRDTLFSFHPVSETFLQRMMSLYVASHYKNSPNDLQLMSDAPAHHLFVLLPPIKEGDNSLPDPLCVVQVCLEGEISKQTVLYSLSRGQQPSGDLIPWLISQQFQDDDFANLSGARIVRIATHPDYVKMGYGSRCLELLTSFYQGEFSALNENENYQQESIVRVDDAELENADLRNEEIKIRDPRKMPPLLLKLSEKRPVRLHYLGVSFGLTSQLHKFWKRAGFVPLYLRQTPNNLTGENTCVMLKALKSDDLVTTCDPGWLAAFSKDFHKRFLNLLSYNFRNFPSVLSLSIMEAVDAGNDANKRVQSFNKSALESYLSVYDLKRLESYSNNMLDYHVIIDLLPTIAYLYFSRRLGDIKLSGVQSSILLGIGLQRKNIDDLEKELTLPSNQILALFIKIIRKFSTYFRSLETQAIQKEIPDETTVVKKKNVEKISKQKTTIEESMKSGLNYNENDEASWDPVSKTLDEDLNEAGEEVISQMIETQRELINSLDLSKYAISGTPESWEEAQTKIASGKQNISTIVSIKNLESTKKRRAIETVTDIVNKEFKMSKREGKKTKKSKK","length":1090,"molWeight":123090,"crc64":"1C2060FA0D18F69C","md5":"A14D6A4A3665262DFC9B18371D246A1A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":4,"Binding site":5},"uniParcId":"UPI000ED9DFE8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397S9H1","uniProtkbId":"A0A397S9H1_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":32,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA79371.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034808"}],"value":"DNA 3'-5' helicase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034808"}],"value":"5.6.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00078607"}],"value":"DNA repair helicase RAD25"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00076598"}],"value":"RNA polymerase II transcription factor B subunit SSL2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075489"}],"value":"Suppressor of stem-loop mutation 2"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA79371.1"}],"value":"C1645_840852"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058901"}],"value":"ATP-dependent 3'-5' DNA helicase/translocase; binds dsDNA rather than ssDNA, unzipping it in a translocase rather than classical helicase activity. Component of the general transcription and DNA repair factor IIH (TFIIH) core complex. When complexed to CDK-activating kinase (CAK), involved in RNA transcription by RNA polymerase II. Also involved in transcription-coupled nucleotide excision repair (NER) of damaged DNA. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/SSL2, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/SSL2 is required for promoter opening and promoter escape"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048988"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.","ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034617"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011640"}],"value":"Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006637"}],"value":"Belongs to the helicase family. RAD25/XPB subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA79371.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":521,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51192"}]},{"type":"Domain","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":736,"modifier":"EXACT"}},"description":"Helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51194"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":809,"modifier":"EXACT"},"end":{"value":844,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":821,"modifier":"EXACT"},"end":{"value":834,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":844,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA79371.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA79371.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01001340","properties":[{"key":"ProteinId","value":"RIA79371.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397S9H1","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397S9H1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"10262986at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0000112","properties":[{"key":"GoTerm","value":"C:nucleotide-excision repair factor 3 complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005675","properties":[{"key":"GoTerm","value":"C:transcription factor TFIIH holo complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0097550","properties":[{"key":"GoTerm","value":"C:transcription preinitiation complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043138","properties":[{"key":"GoTerm","value":"F:3'-5' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016787","properties":[{"key":"GoTerm","value":"F:hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006289","properties":[{"key":"GoTerm","value":"P:nucleotide-excision repair"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006367","properties":[{"key":"GoTerm","value":"P:transcription initiation at RNA polymerase II promoter"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd18029","properties":[{"key":"EntryName","value":"DEXHc_XPB"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18789","properties":[{"key":"EntryName","value":"SF2_C_XPB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000077","properties":[{"key":"EntryName","value":"Probable DNA repair helicase RAD25"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000117","properties":[{"key":"EntryName","value":"Putative DNA repair helicase rad25"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR050615","properties":[{"key":"EntryName","value":"ATP-dep_DNA_Helicase"}]},{"database":"InterPro","id":"IPR032438","properties":[{"key":"EntryName","value":"ERCC3_RAD25_C"}]},{"database":"InterPro","id":"IPR006935","properties":[{"key":"EntryName","value":"Helicase/UvrB_N"}]},{"database":"InterPro","id":"IPR014001","properties":[{"key":"EntryName","value":"Helicase_ATP-bd"}]},{"database":"InterPro","id":"IPR001650","properties":[{"key":"EntryName","value":"Helicase_C-like"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR001161","properties":[{"key":"EntryName","value":"XPB/Ssl2"}]},{"database":"InterPro","id":"IPR032830","properties":[{"key":"EntryName","value":"XPB/Ssl2_N"}]},{"database":"NCBIfam","id":"TIGR00603","properties":[{"key":"EntryName","value":"rad25"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11274:SF0","properties":[{"key":"EntryName","value":"GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11274","properties":[{"key":"EntryName","value":"RAD25/XP-B DNA REPAIR HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16203","properties":[{"key":"EntryName","value":"ERCC3_RAD25_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13625","properties":[{"key":"EntryName","value":"Helicase_C_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04851","properties":[{"key":"EntryName","value":"ResIII"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00851","properties":[{"key":"EntryName","value":"XRODRMPGMNTB"}]},{"database":"SMART","id":"SM00487","properties":[{"key":"EntryName","value":"DEXDc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00490","properties":[{"key":"EntryName","value":"HELICc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51192","properties":[{"key":"EntryName","value":"HELICASE_ATP_BIND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51194","properties":[{"key":"EntryName","value":"HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPPTSKRRFRDDDEYLPSGPSRSNKKSRKFSSKKSNSATPNIINSEDENDLTLTKEALIPKSAVIDIDSISSTLNVNIPRDSVSKYFGEDDFSYIKLKKDHANRPLWINPNTGHIILEGFSPFAEKAQDFLITISEPVSRPSHIHEYKLTPYSLYAAVSVGLETEAIIDVLRILSKIEIPDSIMELIRTCTLSYGKVKLVLKHNRYFVESSYADILQKLLQDKDIAEARVVNSEGSDNEGFLKDRAPTSKDLIISGKKVQEKETDTDGKSSEPITEDDNLFNAVVQIDKEDEEEEEDEVHSFEIKSEKFEVVKKRCIELDYPMLEEYDFRNDSTLPQLDIDLKPITVIRPYQEKCLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSCLVLCTSAVSVMQWKQQFLTWSNIKESQIAVFTSDMKEKFSGQSGIVISTYSMVANTRTRSYDAGKMMEFITGREWGFILLDEVHVVPANMFRKVVTTIAAHTKLGLTATLVREDDKIGDLNFLIGPKLYEANWMDLASKGHIANVQCAEVWCPMTPEFYAQYLKATSRKRMLLYAMNPNKFQACQYLIRFHEERGDKIIVFSDNVYALEKYARQLKVPFIHGKTKPPERMYILNLFQHDPKVNTIFLSKVGDTSIDLPEATCLIQISSHYGSRRQEAQRLGRILRAKRRNDEGFNAFFYSLVSTDTQEMYYSTKRQQFLIDQGYAFKVITKLEGMDTATDLVYRTPSEQMSLLTEVLLANDNDADLDNDIESNADDLPGVVTSRNFTSQQKGYGGVKRSVGSMKSLSGADDMAYMELSSSSSSPRTMKKVDKKTQAKDHHPLFKKQWLKGR","length":844,"molWeight":95671,"crc64":"B61DB9FD2C31EB3B","md5":"650D78DC2C117CBC298F3E0D66EFBAB1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Compositional bias":3},"uniParcId":"UPI000ED23D10"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397S9N9","uniProtkbId":"A0A397S9N9_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-12-05","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81529.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Ribokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"RK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"2.7.1.15"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81529.1"}],"value":"C1645_700734"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribose + ATP = D-ribose 5-phosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13697"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:47013"},{"database":"ChEBI","id":"CHEBI:78346"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.15","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81529.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"Carbohydrate kinase PfkB","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00294"}]},{"type":"Active site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00117"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03215"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81529.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81529.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000782","properties":[{"key":"ProteinId","value":"RIA81529.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397S9N9","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397S9N9","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"415590at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00916","properties":[{"key":"RectionId","value":"UER00889"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004747","properties":[{"key":"GoTerm","value":"F:ribokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046835","properties":[{"key":"GoTerm","value":"P:carbohydrate phosphorylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019303","properties":[{"key":"GoTerm","value":"P:D-ribose catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01174","properties":[{"key":"EntryName","value":"ribokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01987","properties":[{"key":"EntryName","value":"Ribokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011611","properties":[{"key":"EntryName","value":"PfkB_dom"}]},{"database":"InterPro","id":"IPR002139","properties":[{"key":"EntryName","value":"Ribo/fructo_kinase"}]},{"database":"InterPro","id":"IPR011877","properties":[{"key":"EntryName","value":"Ribokinase"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"PANTHER","id":"PTHR10584:SF166","properties":[{"key":"EntryName","value":"RIBOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10584","properties":[{"key":"EntryName","value":"SUGAR KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00294","properties":[{"key":"EntryName","value":"PfkB"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00990","properties":[{"key":"EntryName","value":"RIBOKINASE"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50084","properties":[{"key":"EntryName","value":"KH_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEESKILTFGSINIDEFFEVPHIVSSGETITSSKYTQRAGGKGANQSVSLAKAGALIWHAGKIGRDGAWIKEYMSEFGVKVDHIIISEDQPTGRAFIQVSQKTRDNSIVLLPGTNHMINLDEARKVLSQEFDLVIMQNEIGQIGGEILKLCKEKGLTTVFNPAPISEDIINVFSFNLVDYLIVNKLEADQLYKQISESDKKDISVQDLLTSISNEFKQLIGIIITLGSEGLYAWYKPEQKMFYLPAFKTEVLDTTGAGDTFIGYFVSGIVRNLKHERRVDSNVILPTSETFLNALKEATVAASLAVGQLGAMESIPSFIDVQKSKIMFDD","length":330,"molWeight":36512,"crc64":"599BC3A9262799AC","md5":"9E36480F55C17D4E5A13CAA71CD7D13F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":13},"uniParcId":"UPI000ECC7D76"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397S9W3","uniProtkbId":"A0A397S9W3_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-12-05","entryVersion":30,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA83110.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Phospholipid-transporting ATPase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"7.6.2.1"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA83110.1"}],"value":"C1645_797880"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.","ecNumber":"7.6.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034036"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66132"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:64612"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049128"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66133"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049128"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008109"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA83110.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1051,"modifier":"EXACT"},"end":{"value":1072,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1084,"modifier":"EXACT"},"end":{"value":1104,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1134,"modifier":"EXACT"},"end":{"value":1155,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1175,"modifier":"EXACT"},"end":{"value":1192,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1199,"modifier":"EXACT"},"end":{"value":1217,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1248,"modifier":"EXACT"},"end":{"value":1266,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Domain","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"P-type ATPase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF16209"}]},{"type":"Domain","location":{"start":{"value":1020,"modifier":"EXACT"},"end":{"value":1276,"modifier":"EXACT"}},"description":"P-type ATPase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF16212"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":686,"modifier":"EXACT"},"end":{"value":755,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1302,"modifier":"EXACT"},"end":{"value":1331,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1400,"modifier":"EXACT"},"end":{"value":1423,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":686,"modifier":"EXACT"},"end":{"value":717,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":725,"modifier":"EXACT"},"end":{"value":748,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1317,"modifier":"EXACT"},"end":{"value":1328,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"4-aspartylphosphate intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-1"}]},{"type":"Binding site","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":408,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":408,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":592,"modifier":"EXACT"},"end":{"value":592,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":647,"modifier":"EXACT"},"end":{"value":647,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":670,"modifier":"EXACT"},"end":{"value":670,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":799,"modifier":"EXACT"},"end":{"value":799,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":879,"modifier":"EXACT"},"end":{"value":879,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":880,"modifier":"EXACT"},"end":{"value":880,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":881,"modifier":"EXACT"},"end":{"value":881,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":967,"modifier":"EXACT"},"end":{"value":967,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":973,"modifier":"EXACT"},"end":{"value":973,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":994,"modifier":"EXACT"},"end":{"value":994,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":997,"modifier":"EXACT"},"end":{"value":997,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":998,"modifier":"EXACT"},"end":{"value":998,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":998,"modifier":"EXACT"},"end":{"value":998,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA83110.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA83110.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000597","properties":[{"key":"ProteinId","value":"RIA83110.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"STRING","id":"658196.A0A397S9W3","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"377733at2759","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005802","properties":[{"key":"GoTerm","value":"C:trans-Golgi network"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0140326","properties":[{"key":"GoTerm","value":"F:ATPase-coupled intramembrane lipid carrier activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0032456","properties":[{"key":"GoTerm","value":"P:endocytic recycling"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0045332","properties":[{"key":"GoTerm","value":"P:phospholipid translocation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006892","properties":[{"key":"GoTerm","value":"P:post-Golgi vesicle-mediated transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd02073","properties":[{"key":"EntryName","value":"P-type_ATPase_APLT_Dnf-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1000:FF:000172","properties":[{"key":"EntryName","value":"Phospholipid-transporting ATPase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1110.10","properties":[{"key":"EntryName","value":"Calcium-transporting ATPase, cytoplasmic domain N"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.70.150.10","properties":[{"key":"EntryName","value":"Calcium-transporting ATPase, cytoplasmic transduction domain A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1000","properties":[{"key":"EntryName","value":"HAD superfamily/HAD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023299","properties":[{"key":"EntryName","value":"ATPase_P-typ_cyto_dom_N"}]},{"database":"InterPro","id":"IPR018303","properties":[{"key":"EntryName","value":"ATPase_P-typ_P_site"}]},{"database":"InterPro","id":"IPR023298","properties":[{"key":"EntryName","value":"ATPase_P-typ_TM_dom_sf"}]},{"database":"InterPro","id":"IPR008250","properties":[{"key":"EntryName","value":"ATPase_P-typ_transduc_dom_A_sf"}]},{"database":"InterPro","id":"IPR036412","properties":[{"key":"EntryName","value":"HAD-like_sf"}]},{"database":"InterPro","id":"IPR023214","properties":[{"key":"EntryName","value":"HAD_sf"}]},{"database":"InterPro","id":"IPR006539","properties":[{"key":"EntryName","value":"P-type_ATPase_IV"}]},{"database":"InterPro","id":"IPR032631","properties":[{"key":"EntryName","value":"P-type_ATPase_N"}]},{"database":"InterPro","id":"IPR001757","properties":[{"key":"EntryName","value":"P_typ_ATPase"}]},{"database":"InterPro","id":"IPR032630","properties":[{"key":"EntryName","value":"P_typ_ATPase_c"}]},{"database":"InterPro","id":"IPR044492","properties":[{"key":"EntryName","value":"P_typ_ATPase_HD_dom"}]},{"database":"NCBIfam","id":"TIGR01652","properties":[{"key":"EntryName","value":"ATPase-Plipid"},{"key":"MatchStatus","value":"2"}]},{"database":"NCBIfam","id":"TIGR01494","properties":[{"key":"EntryName","value":"ATPase_P-type"},{"key":"MatchStatus","value":"2"}]},{"database":"PANTHER","id":"PTHR24092:SF174","properties":[{"key":"EntryName","value":"PHOSPHOLIPID-TRANSPORTING ATPASE DNF3-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24092","properties":[{"key":"EntryName","value":"PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13246","properties":[{"key":"EntryName","value":"Cation_ATPase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00702","properties":[{"key":"EntryName","value":"Hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16212","properties":[{"key":"EntryName","value":"PhoLip_ATPase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16209","properties":[{"key":"EntryName","value":"PhoLip_ATPase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00119","properties":[{"key":"EntryName","value":"CATATPASE"}]},{"database":"SFLD","id":"SFLDG00002","properties":[{"key":"EntryName","value":"C1.7:_P-type_atpase_like"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00003","properties":[{"key":"EntryName","value":"Haloacid_Dehalogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00027","properties":[{"key":"EntryName","value":"p-type_atpase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81653","properties":[{"key":"EntryName","value":"Calcium ATPase, transduction domain A"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81665","properties":[{"key":"EntryName","value":"Calcium ATPase, transmembrane domain M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56784","properties":[{"key":"EntryName","value":"HAD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81660","properties":[{"key":"EntryName","value":"Metal cation-transporting ATPase, ATP-binding domain N"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00154","properties":[{"key":"EntryName","value":"ATPASE_E1_E2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIPGGHNQDDAGREIPINPNNQVPLIDPRTKKPFINNSITTSRYKIYNFIPKQLIYQFSKIANVYFLFVAILQSIPGFSPTGRFTTIIPLSVFMSIAIAHEGFDDYRRHKQDQIENNKECSVLNVYKSNDSTTQHLGVWRKTKWRNLKVGDLVSVKAQEWIPADLLLLHSTGEEGTCYIETAALDGETNLKQRQALKETNSIVTSPEALADFRATVHTENPNQDLYNFDGSITLANKKTISLTNNQILLRGTILRNTPEIYGLVIFTGEETKLRMNASKNIRTKAPSIQKLMNKVVIIIFCFVMFLATMSTIFSKLWDADFGDDSFYLHTEINQMDILQTLASYIILFNTMIPISLYVTMEVVKLAQAYFINNDLEMYHQETDTPAEARTSTINEELGQVSYLFSDKTGTLTDNVMLFRKISVGGRAFIHDLDLRRIEEDDLLRMMKQPQKSNTIQGIFKRFSLSTRRHNRSHTRDDTNDGDDIAFENRQLNRSDSTRSGRFSMIAPNSIGPSPLYRRDSTSGVSLKSVKGKTGQHMKSTLDLLTILHHQNNTPFYEKARFFLLAVALCHTCVPEIDQETQDIFYQAASPDEFALVTAAKELGYVVMDRSMSSVSLRVNNDGPNGLKVPNSATTMYETYKILNVIEFSSKRKRMSIIYRLPDGRICLLCKGADSIVLERLRDPVKRSDKKEKYNEDKSYEQKNESKFEKRPLHDLRVDTSIVDRSSNNQSGSSVISSNPNTPKTPSSPVSIKRAHERSYSIRTVDSERSVVDLFPMRDDTWLYSQTMCHIQDFATEGLRTLLYAHRFMDEEEYTSWNDLYQEASTSLVDRQQKLEEVAELIERDLEITGATAIEDKLQNGVPETIDKLRRAGIRVWMLTGDKRETAINIGYSCSLIKDYSTTIIIDSNVEDLKSMMKRTLKDVKNGKAKHPVAVVDGATLMKIEKDQDIMEIFVDLGILCEAVICCRVSPSQKALVVRNIRSKLTNHVTLAIGDGANDIAMIQEAHVGIGITGREGLQAARSSDYSIAQFRFLSNLLFVHGRWSYVRVSKFVLGTFYKCMCFYLTQGLFQLFTGFSATSLYEQWTLSFYNTLFSSLPVIVIGMFEKDLNMKTTIGVPELYNLGQRNGGFNLQLFFTWMGAGIFHACAIIGIPFIIHGFLEEGELGRFGSPQLYELGMTVYSCVVFVVTIKIAYLECHNWTWITHITSILTLIGWYLYQTIYSFLYPKSSGQVYDVNGTFQRVGSKSEYWATILLTVSIAMLPNLLVKVIKNIILPTDVDIYQEIEKDKKLLDKLIEGGNDSNKDDDIEGGFKRHIKRNENKSSKKDNIKTGSSEYNNIKEVNVDNIVSKIPSVTSNFNQQNGNSSPTSTAISTAISNTTTLSPHSPVRRLRSTNSLDEFTFPKQDNEQNNDEIPPPSYHADTITPKTSFESFGHLNNGNNGSNMETLIEETEDDLQSKRNSDNII","length":1465,"molWeight":165961,"crc64":"C85CFB7DABCF8EF8","md5":"9E5B941F20F08019DF85D55709DDF587"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":10,"Domain":2,"Region":4,"Compositional bias":3,"Active site":1,"Binding site":18},"uniParcId":"UPI000EC6175D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A397S9Y7","uniProtkbId":"A0A397S9Y7_9GLOM","entryAudit":{"firstPublicDate":"2018-12-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-12-05","entryVersion":33,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Glomus cerebriforme","taxonId":658196,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81125.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"lineage":["Eukaryota","Fungi","Fungi incertae sedis","Glomeromycota","Glomeromycotina","Glomeromycetes","Glomerales","Glomeraceae","Glomus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}],"value":"Threonine dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}],"value":"4.3.1.19"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}],"value":"Threonine deaminase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81125.1"}],"value":"C1645_729838"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonine = 2-oxobutanoate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22108"},{"database":"ChEBI","id":"CHEBI:16763"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:57926"}],"ecNumber":"4.3.1.19","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001274"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004810"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}],"value":"Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004173"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010869"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}],"value":"Belongs to the serine/threonine dehydratase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81125.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":452,"modifier":"EXACT"}},"description":"ACT-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51672"}]},{"type":"Domain","location":{"start":{"value":474,"modifier":"EXACT"},"end":{"value":545,"modifier":"EXACT"}},"description":"ACT-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51672"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023304"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}],"id":"KW-0100","category":"Biological process","name":"Branched-chain amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022624"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}],"id":"KW-0412","category":"Biological process","name":"Isoleucine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362012"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EP048H7PPJJEF","citationType":"submission","authors":["Morin E.","San Clemente H.","Chen E.C.H.","De La Providencia I.","Hainaut M.","Kuo A.","Kohler A.","Murat C.","Tang N.","Roy S.","Loubradou J.","Henrissat B.","Grigoriev I.V.","Corradi N.","Roux C.","Martin F.M."],"title":"Comparative genomics reveals the genomic features of Rhizophagus irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their symbiotic lifestyle signature.","publicationDate":"JUN-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81125.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}],"value":"DAOM 227022","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"RIA81125.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000265703"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QKYT01000842","properties":[{"key":"ProteinId","value":"RIA81125.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A397S9Y7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"658196.A0A397S9Y7","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"4418812at2759","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00047","properties":[{"key":"RectionId","value":"UER00054"}]},{"database":"Proteomes","id":"UP000265703","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003941","properties":[{"key":"GoTerm","value":"F:L-serine ammonia-lyase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004794","properties":[{"key":"GoTerm","value":"F:threonine deaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:1901705","properties":[{"key":"GoTerm","value":"P:L-isoleucine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006565","properties":[{"key":"GoTerm","value":"P:L-serine catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006567","properties":[{"key":"GoTerm","value":"P:L-threonine catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04906","properties":[{"key":"EntryName","value":"ACT_ThrD-I_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04907","properties":[{"key":"EntryName","value":"ACT_ThrD-I_2"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01562","properties":[{"key":"EntryName","value":"Thr-dehyd"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1020.10:FF:000001","properties":[{"key":"EntryName","value":"L-threonine dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1100:FF:000008","properties":[{"key":"EntryName","value":"L-threonine dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1100:FF:000005","properties":[{"key":"EntryName","value":"Threonine dehydratase catabolic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.1020.10","properties":[{"key":"EntryName","value":"Biosynthetic Threonine Deaminase, Domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045865","properties":[{"key":"EntryName","value":"ACT-like_dom_sf"}]},{"database":"InterPro","id":"IPR050147","properties":[{"key":"EntryName","value":"Ser/Thr_Dehydratase"}]},{"database":"InterPro","id":"IPR000634","properties":[{"key":"EntryName","value":"Ser/Thr_deHydtase_PyrdxlP-BS"}]},{"database":"InterPro","id":"IPR001721","properties":[{"key":"EntryName","value":"TD_ACT-like"}]},{"database":"InterPro","id":"IPR038110","properties":[{"key":"EntryName","value":"TD_ACT-like_sf"}]},{"database":"InterPro","id":"IPR005787","properties":[{"key":"EntryName","value":"Thr_deHydtase_biosynth"}]},{"database":"InterPro","id":"IPR001926","properties":[{"key":"EntryName","value":"TrpB-like_PALP"}]},{"database":"InterPro","id":"IPR036052","properties":[{"key":"EntryName","value":"TrpB-like_PALP_sf"}]},{"database":"NCBIfam","id":"NF006674","properties":[{"key":"EntryName","value":"ilvA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01124","properties":[{"key":"EntryName","value":"ilvA_2Cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48078:SF11","properties":[{"key":"EntryName","value":"THREONINE DEHYDRATASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48078","properties":[{"key":"EntryName","value":"THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00291","properties":[{"key":"EntryName","value":"PALP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00585","properties":[{"key":"EntryName","value":"Thr_dehydrat_C"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF55021","properties":[{"key":"EntryName","value":"ACT-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53686","properties":[{"key":"EntryName","value":"Tryptophan synthase beta subunit-like PLP-dependent enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51672","properties":[{"key":"EntryName","value":"ACT_LIKE"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00165","properties":[{"key":"EntryName","value":"DEHYDRATASE_SER_THR"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVKNDTQNNASQEYQSRTNNVSYPLPSGRALVETDTTLPSPHLSNQISNLPKPDYLRLILTSRVYEIVKETPLQYAVNLSLKTQNNVYLKREDLQEVFSFKIRGAYNKIAHLSDEERKRGVIACSAGNHAQGVAMSAKHLGLPATIVMPLATPAIKWRNVKRLGSKVVLHGNDFDEAKQECARLSEIEQLTNIPPYDDPYVIAGQGTIAMEIIRQHNVNDIDAIFACVGGGGLLAGIGSYIKRLCPKIKIIGVETYDANAMYLSLKEKKRVTLEEVGLFADGAAVKIVGEETFRVCSEVVDEMIMVSTDEICAAIKDIFEDTRSIVEPAGALGVAGIKKYIAENNIKGETFVAVTSGANMNFDRLRFVAERADLGEQREVLISVIIPERPGSFVKLYNQIHPRPITEFSYRFSDSEKAWIYTSFMVENREQEISEILQNLKDNGMSGQDISDNEMAKSHARYLVGGRSKVENERLYRFEFPERPGALQKFLLGLRIDWNISLFHYRNHGSDIGKVLVGVQVPSQDFEAFEIFKNNLGYHVVEETDNPVYKQFLI","length":554,"molWeight":62150,"crc64":"1A1D4EDCFD1A1387","md5":"B73417ACC4E7420B2014A57E9379707A"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":2},"uniParcId":"UPI000EED1DF9"}}]}