{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q59490","uniProtkbId":"RTPR_LACLE","entryAudit":{"firstPublicDate":"2003-09-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-01-23","entryVersion":105,"sequenceVersion":4},"annotationScore":5.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase"},"shortNames":[{"value":"RTPR"}],"ecNumbers":[{"value":"1.17.4.2"}]}},"genes":[{"geneName":{"value":"rtpR"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 2'-deoxyribonucleoside 5'-triphosphate + [thioredoxin]-disulfide + H2O = a ribonucleoside 5'-triphosphate + [thioredoxin]-dithiol","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12701"},{"database":"Rhea","id":"RHEA-COMP:10698"},{"database":"Rhea","id":"RHEA-COMP:10700"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:50058"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:61560"}],"ecNumber":"1.17.4.2"}},{"commentType":"COFACTOR","cofactors":[{"name":"adenosylcob(III)alamin","cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18408"}}]},{"texts":[{"value":"Allosterically regulated by ATP and dNTP"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11875520"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the class II ribonucleoside-triphosphate reductase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8397403"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":739,"modifier":"EXACT"}},"description":"Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase","featureId":"PRO_0000221428"},{"type":"Region","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"Effector region-1"},{"type":"Region","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"Effector region-2"},{"type":"Region","location":{"start":{"value":565,"modifier":"EXACT"},"end":{"value":626,"modifier":"EXACT"}},"description":"Adenosylcobalamin-binding-1"},{"type":"Region","location":{"start":{"value":685,"modifier":"EXACT"},"end":{"value":724,"modifier":"EXACT"}},"description":"Adenosylcobalamin-binding-2"},{"type":"Active site","location":{"start":{"value":408,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":""},{"type":"Active site","location":{"start":{"value":410,"modifier":"EXACT"},"end":{"value":410,"modifier":"EXACT"}},"description":""},{"type":"Disulfide bond","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"Redox-active"},{"type":"Sequence conflict","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"in Ref. 1; AAA03078","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["C"]}},{"type":"Sequence conflict","location":{"start":{"value":717,"modifier":"EXACT"},"end":{"value":717,"modifier":"EXACT"}},"description":"in Ref. 1; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["D"]}},{"type":"Helix","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Turn","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Turn","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Turn","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Turn","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Turn","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":340,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":350,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":386,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Turn","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":402,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":424,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":426,"modifier":"EXACT"},"end":{"value":431,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":450,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":458,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":471,"modifier":"EXACT"},"end":{"value":474,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":477,"modifier":"EXACT"},"end":{"value":485,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":489,"modifier":"EXACT"},"end":{"value":497,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Turn","location":{"start":{"value":499,"modifier":"EXACT"},"end":{"value":501,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":504,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":512,"modifier":"EXACT"},"end":{"value":536,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":545,"modifier":"EXACT"},"end":{"value":547,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":551,"modifier":"EXACT"},"end":{"value":557,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":569,"modifier":"EXACT"},"end":{"value":578,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":583,"modifier":"EXACT"},"end":{"value":589,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":593,"modifier":"EXACT"},"end":{"value":596,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":598,"modifier":"EXACT"},"end":{"value":600,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":603,"modifier":"EXACT"},"end":{"value":611,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Turn","location":{"start":{"value":613,"modifier":"EXACT"},"end":{"value":616,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Turn","location":{"start":{"value":623,"modifier":"EXACT"},"end":{"value":625,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":628,"modifier":"EXACT"},"end":{"value":641,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":650,"modifier":"EXACT"},"end":{"value":653,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":655,"modifier":"EXACT"},"end":{"value":660,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":661,"modifier":"EXACT"},"end":{"value":667,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Turn","location":{"start":{"value":668,"modifier":"EXACT"},"end":{"value":671,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":673,"modifier":"EXACT"},"end":{"value":679,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Beta strand","location":{"start":{"value":689,"modifier":"EXACT"},"end":{"value":692,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":695,"modifier":"EXACT"},"end":{"value":704,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]},{"type":"Helix","location":{"start":{"value":709,"modifier":"EXACT"},"end":{"value":719,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L1L"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"id":"KW-0846","category":"Ligand","name":"Cobalamin"},{"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0676","category":"Domain","name":"Redox-active center"}],"references":[{"referenceNumber":1,"citation":{"id":"8397403","citationType":"journal article","authors":["Booker S.","Stubbe J."],"citationCrossReferences":[{"database":"PubMed","id":"8397403"},{"database":"DOI","id":"10.1073/pnas.90.18.8352"}],"title":"Cloning, sequencing, and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii.","publicationDate":"1993","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"8352","lastPage":"8356","volume":"90"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-22; 112-121; 449-461; 489-513 AND 702-739"]},{"referenceNumber":2,"citation":{"id":"3322391","citationType":"journal article","authors":["Lin A.-N.I.","Ashley G.W.","Stubbe J."],"citationCrossReferences":[{"database":"PubMed","id":"3322391"},{"database":"DOI","id":"10.1021/bi00396a006"}],"title":"Location of the redox-active thiols of ribonucleotide reductase: sequence similarity between the Escherichia coli and Lactobacillus leichmannii enzymes.","publicationDate":"1987","journal":"Biochemistry","firstPage":"6905","lastPage":"6909","volume":"26"},"referencePositions":["PROTEIN SEQUENCE OF 112-121 AND 722-739"],"referenceComments":[{"value":"ATCC 7830","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"11875520","citationType":"journal article","authors":["Sintchak M.D.","Arjara G.","Kellogg B.A.","Stubbe J.","Drennan C.L."],"citationCrossReferences":[{"database":"PubMed","id":"11875520"},{"database":"DOI","id":"10.1038/nsb774"}],"title":"The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer.","publicationDate":"2002","journal":"Nat. Struct. Biol.","firstPage":"293","lastPage":"300","volume":"9"},"referencePositions":["X-RAY CRYSTALLOGRAPHY","X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ADENINYLPENTYLCOBALAMIN","SEQUENCE REVISION TO 151"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"L20047","properties":[{"key":"ProteinId","value":"AAA03078.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Unassigned_DNA"}]},{"database":"RefSeq","id":"WP_035184117.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000054.1"}]},{"database":"PDB","id":"1L1L","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.75 A"},{"key":"Chains","value":"A/B/C/D=1-739"}]},{"database":"AlphaFoldDB","id":"Q59490","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q59490","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.17.4.2","properties":[{"key":"OrganismId","value":"2878"}]},{"database":"SABIO-RK","id":"Q59490","properties":[{"key":"Description","value":"-"}]},{"database":"EvolutionaryTrace","id":"Q59490","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0031419","properties":[{"key":"GoTerm","value":"F:cobalamin binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000166","properties":[{"key":"GoTerm","value":"F:nucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004748","properties":[{"key":"GoTerm","value":"F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008998","properties":[{"key":"GoTerm","value":"F:ribonucleoside-triphosphate reductase (thioredoxin) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006260","properties":[{"key":"GoTerm","value":"P:DNA replication"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01676","properties":[{"key":"EntryName","value":"RNR_II_monomer"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.70.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1620.10","properties":[{"key":"EntryName","value":"b-12 dependent (class ii) ribonucleotide reductase, Chain A, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1390.10","properties":[{"key":"EntryName","value":"b-12 dependent (class ii) ribonucleotide reductase, chain A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050862","properties":[{"key":"EntryName","value":"RdRp_reductase_class-2"}]},{"database":"InterPro","id":"IPR054158","properties":[{"key":"EntryName","value":"RNR-II_ins_dom"}]},{"database":"InterPro","id":"IPR040763","properties":[{"key":"EntryName","value":"RNR_alpha_hel"}]},{"database":"InterPro","id":"IPR013345","properties":[{"key":"EntryName","value":"RTP_Rdtase_AdoCbl-dep"}]},{"database":"NCBIfam","id":"TIGR02505","properties":[{"key":"EntryName","value":"RTPR"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43371:SF1","properties":[{"key":"EntryName","value":"RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43371","properties":[{"key":"EntryName","value":"VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21995","properties":[{"key":"EntryName","value":"RNR-II_ins_dom"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17975","properties":[{"key":"EntryName","value":"RNR_Alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51998","properties":[{"key":"EntryName","value":"PFL-like glycyl radical enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSEEISLSAEFIDRVKASVKPHWGKLGWVTYKRTYARWLPEKGRSENWDETVKRVVEGNINLDPRLQDSPSLELKQSLTEEAERLYKLIYGLGATPSGRNLWISGTDYQRRTGDSLNNCWFVAIRPQKYGDSKIVPSYLGKQEKAVSMPFSFLFDELMKGGGVGFSVARSNISQIPRVDFAIDLQLVVDETSESYDASVKVGAVGKNELVQDADSIYYRLPDTREGWVLANALLIDLHFAQTNPDRKQKLILDLSDIRPYGAEIHGFGGTASGPMPLISMLLDVNEVLNNKAGGRLTAVDAADICNLIGKAVVAGNVRRSAELALGSNDDQDFISMKQDQEKLMHHRWASNNSVAVDSAFSGYQPIAAGIRENGEPGIVNLDLSKNYGRIVDGYQAGIDGDVEGTNPCGEISLANGEPCNLFEVFPLIAEEQGWDLQEVFALAARYAKRVTFSPYDWEISREIIQKNRRIGISMSGIQDWLLTRLGNRVVTGFKDDFDPETHEAIKVPVYDKRAIKMVDQLYKAVVKADQDYSKTLGCNESIKHTTVKPSGTVAKLAGASEGMHFHYGAYLIQRIRFQDSDPLLPALKACGYRTEADIYTENTTCVEFPIKAVGADNPNFASAGTVSIAEQFATQAFLQTYWSDNAVSCTITFQDSEGDQVESLLRQYRFITKSTSLLPYFGGSLQQAPKEPIDKETYEKRSQEITGNVEEVFSQLNSDVKDLELVDQTDCEGGACPIK","length":739,"molWeight":81983,"crc64":"8B04C6A5EADB6D6E","md5":"A60D2D5CD23EE0EB02BA812BA5BF7511"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Region":4,"Active site":2,"Disulfide bond":1,"Sequence conflict":2,"Helix":33,"Turn":10,"Beta strand":24},"uniParcId":"UPI00001122E2"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9R5V5","uniProtkbId":"NTD_LACLE","entryAudit":{"firstPublicDate":"2004-09-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-01-23","entryVersion":80,"sequenceVersion":3},"annotationScore":4.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000305"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Nucleoside deoxyribosyltransferase"},"shortNames":[{"value":"N-deoxyribosyltransferase"}],"ecNumbers":[{"value":"2.4.2.6"}]}},"genes":[{"geneName":{"value":"ntd"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7797550"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8805514"}],"value":"Catalyzes the cleavage of the glycosidic bond of 2'-deoxyribonucleosides and the transfer of the deoxyribosyl moiety to an acceptor purine or pyrimidine base"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-deoxy-D-ribosyl-base(1) + base(2) = 2-deoxy-D-ribosyl-base(2) + base(1).","ecNumber":"2.4.2.6","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7797550"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","phDependence":{"texts":[{"value":"Optimum pH is 6.0."}]}},{"texts":[{"value":"Nucleotide metabolism; nucleotide salvage pathway"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8805514"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the nucleoside deoxyribosyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7797550"}],"value":"Was originally thought to originate from E.coli"}],"commentType":"CAUTION"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7797550"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Nucleoside deoxyribosyltransferase","featureId":"PRO_0000220067"},{"type":"Active site","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7797550"}]},{"type":"Mutagenesis","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Loss of transferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7797550"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Beta strand","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Helix","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Helix","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F08"}]},{"type":"Helix","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Helix","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Turn","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Helix","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Helix","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Beta strand","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Helix","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1F8Y"}]},{"type":"Helix","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Beta strand","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Helix","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Helix","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Beta strand","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]},{"type":"Helix","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9F09"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0546","category":"Biological process","name":"Nucleotide metabolism"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"7797550","citationType":"journal article","authors":["Porter D.J.T.","Merrill B.M.","Short S.A."],"citationCrossReferences":[{"database":"PubMed","id":"7797550"},{"database":"DOI","id":"10.1074/jbc.270.26.15551"}],"title":"Identification of the active site nucleophile in nucleoside 2-deoxyribosyltransferase as glutamic acid 98.","publicationDate":"1995","journal":"J. Biol. Chem.","firstPage":"15551","lastPage":"15556","volume":"270"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-26","FUNCTION","ACTIVE SITE","MUTAGENESIS OF GLU-98"],"evidences":[{"evidenceCode":"ECO:0000305"}]},{"referenceNumber":2,"citation":{"id":"8805514","citationType":"journal article","authors":["Armstrong S.R.","Cook W.J.","Short S.A.","Ealick S.E."],"citationCrossReferences":[{"database":"PubMed","id":"8805514"},{"database":"DOI","id":"10.1016/s0969-2126(96)00013-5"}],"title":"Crystal structures of nucleoside 2-deoxyribosyltransferase in native and ligand-bound forms reveal architecture of the active site.","publicationDate":"1996","journal":"Structure","firstPage":"97","lastPage":"107","volume":"4"},"referencePositions":["X-RAY CRYSTALLOGRAPHY"],"evidences":[{"evidenceCode":"ECO:0000305"}]}],"uniProtKBCrossReferences":[{"database":"RefSeq","id":"WP_035184009.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000049.1"}]},{"database":"PDB","id":"1F8X","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"A/B=1-157"}]},{"database":"PDB","id":"1F8Y","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.40 A"},{"key":"Chains","value":"A/B=1-157"}]},{"database":"PDB","id":"4HX9","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.68 A"},{"key":"Chains","value":"A/B/C/D/E/F/G/H=1-157"}]},{"database":"PDB","id":"9EZK","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.79 A"},{"key":"Chains","value":"A/B=1-157"}]},{"database":"PDB","id":"9F08","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.37 A"},{"key":"Chains","value":"A/B=1-157"}]},{"database":"PDB","id":"9F09","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.37 A"},{"key":"Chains","value":"A/B=1-157"}]},{"database":"PDB","id":"9GN2","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.41 A"},{"key":"Chains","value":"A/B=1-157"}]},{"database":"PDB","id":"9GN4","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.48 A"},{"key":"Chains","value":"A/B=1-157"}]},{"database":"AlphaFoldDB","id":"Q9R5V5","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"Q9R5V5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9R5V5","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB03763","properties":[{"key":"GenericName","value":"5-methyl-2'-deoxypseudouridine"}]},{"database":"BRENDA","id":"2.4.2.6","properties":[{"key":"OrganismId","value":"2878"}]},{"database":"UniPathway","id":"UPA00312","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"Q9R5V5","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0050144","properties":[{"key":"GoTerm","value":"F:nucleoside deoxyribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0043173","properties":[{"key":"GoTerm","value":"P:nucleotide salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR007710","properties":[{"key":"EntryName","value":"Nucleoside_deoxyribTrfase"}]},{"database":"Pfam","id":"PF05014","properties":[{"key":"EntryName","value":"Nuc_deoxyrib_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52309","properties":[{"key":"EntryName","value":"N-(deoxy)ribosyltransferase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKKTIYFGAGWFTDRQNKAYKEAMEALKENPTIDLENSYVPLDNQYKGIRVDEHPEYLHDKVWATATYNNDLNGIKTNDIMLGVYIPDEEDVGLGMELGYALSQGKYVLLVIPDEDYGKPINLMSWGVSDNVIKMSQLKDFNFNKPRFDFYEGAVY","length":157,"molWeight":18080,"crc64":"F3CA8CA6F509A91F","md5":"0202D392FAF7A7761104A03A8DC92C19"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Active site":1,"Mutagenesis":1,"Beta strand":4,"Helix":11,"Turn":1},"uniParcId":"UPI00000380F3"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q60252","uniProtkbId":"PYRB_LACLE","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"2004-04-26","entryVersion":96,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Aspartate carbamoyltransferase catalytic subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"value":"2.1.3.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Aspartate transcarbamylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"value":"ATCase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"value":"pyrB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway"}],"commentType":"FUNCTION"},{"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:0000255","source":"HAMAP-Rule","id":"MF_00001"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"},{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"CAA59021.1","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"Aspartate carbamoyltransferase catalytic subunit","featureId":"PRO_0000113147"},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}}],"keywords":[{"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"8725005","citationType":"journal article","authors":["Becker J.","Brendel M."],"citationCrossReferences":[{"database":"PubMed","id":"8725005"},{"database":"DOI","id":"10.1016/0300-9084(96)81323-x"}],"title":"Molecular cloning and characterization of the pyrB gene of Lactobacillus leichmannii encoding aspartate transcarbamylase.","publicationDate":"1996","journal":"Biochimie","firstPage":"3","lastPage":"13","volume":"78"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 4797 / DSM 20076 / BCRC 10699 / JCM 1148 / NBRC 3073 / NCIMB 7854 / 326 / F59","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"8589056","citationType":"journal article","authors":["Schenk-Groeninger R.","Becker J.","Brendel M."],"citationCrossReferences":[{"database":"PubMed","id":"8589056"},{"database":"DOI","id":"10.1016/0300-9084(96)88135-1"}],"title":"Cloning, sequencing, and characterizing the Lactobacillus leichmannii pyrC gene encoding dihydroorotase.","publicationDate":"1995","journal":"Biochimie","firstPage":"265","lastPage":"272","volume":"77"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-336"],"referenceComments":[{"value":"ATCC 4797 / DSM 20076 / BCRC 10699 / JCM 1148 / NBRC 3073 / NCIMB 7854 / 326 / F59","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X84262","properties":[{"key":"ProteinId","value":"CAA59021.1"},{"key":"Status","value":"ALT_INIT"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"X78999","properties":[{"key":"ProteinId","value":"CAA55634.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T46956","properties":[{"key":"EntryName","value":"T46956"}]},{"database":"RefSeq","id":"WP_035184388.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000014.1"}]},{"database":"AlphaFoldDB","id":"Q60252","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q60252","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00116"}]},{"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-UniRule"}]},{"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-UniRule"}]},{"database":"GO","id":"GO:0006520","properties":[{"key":"GoTerm","value":"P:amino acid metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000011","properties":[{"key":"EntryName","value":"Aspartate carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1370","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00001","properties":[{"key":"EntryName","value":"Asp_carb_tr"},{"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":"NCBIfam","id":"TIGR00670","properties":[{"key":"EntryName","value":"asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002032","properties":[{"key":"EntryName","value":"PRK00856.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753:SF6","properties":[{"key":"EntryName","value":"ASPARTATE CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753","properties":[{"key":"EntryName","value":"ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL"},{"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":"SUPFAM","id":"SSF53671","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00097","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTTVSQNQVVVETEDKQDNLLRLPYFVSVEQLSADDVLHLLQRAQYFKNGGEVPALSRPIFCTNMFFENSTRTHTSFEVAERRLGLTVIPFDPSHSSVNKGENLYDTELTMASLGIELSVIRHPENAYYNEIIRPKEGQHLQMGLVNAGDGSGQHPSQSMLDMMTIYNEFGHFDGLKIMIVGDLTNSRVARSNMEILNTLGAEVYFSGPEYWYNAEEFSKYGTYVKNIDDEIPELDVLMLLRVQHERHNGAEAKTEQLFDAKDYNAAYGLNQRRYDMLKDDAIIMHPGPINRGVEWDGDLVEAPKSRYAVQMHNGVFVRMAMIEAVLRGRKLGGLE","length":336,"molWeight":38135,"crc64":"24CFC94AE1F94FB9","md5":"230738EFB96C94FBB6BB36B123C10CB7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"SEQUENCE CAUTION":1},"countByFeatureType":{"Chain":1,"Binding site":10},"uniParcId":"UPI0000358926"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P48795","uniProtkbId":"PYRC_LACLE","entryAudit":{"firstPublicDate":"1996-02-01","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"1996-02-01","entryVersion":108,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"value":"Dihydroorotase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"value":"DHOase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"value":"3.5.2.3"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"value":"pyrC"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"value":"Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24296"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30864"},{"database":"ChEBI","id":"CHEBI:32814"}],"ecNumber":"3.5.2.3","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"value":"Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":427,"modifier":"EXACT"}},"description":"Dihydroorotase","featureId":"PRO_0000147236"},{"type":"Active site","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}]},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"substrate"}}],"keywords":[{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"8589056","citationType":"journal article","authors":["Schenk-Groeninger R.","Becker J.","Brendel M."],"citationCrossReferences":[{"database":"PubMed","id":"8589056"},{"database":"DOI","id":"10.1016/0300-9084(96)88135-1"}],"title":"Cloning, sequencing, and characterizing the Lactobacillus leichmannii pyrC gene encoding dihydroorotase.","publicationDate":"1995","journal":"Biochimie","firstPage":"265","lastPage":"272","volume":"77"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 4797 / DSM 20076 / BCRC 10699 / JCM 1148 / NBRC 3073 / NCIMB 7854 / 326 / F59","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X78999","properties":[{"key":"ProteinId","value":"CAA55633.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T46955","properties":[{"key":"EntryName","value":"T46955"}]},{"database":"RefSeq","id":"WP_035184401.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000014.1"}]},{"database":"AlphaFoldDB","id":"P48795","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P48795","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00117"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004038","properties":[{"key":"GoTerm","value":"F:allantoinase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004151","properties":[{"key":"GoTerm","value":"F:dihydroorotase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006145","properties":[{"key":"GoTerm","value":"P:purine nucleobase catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01317","properties":[{"key":"EntryName","value":"DHOase_IIa"},{"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":"2.30.40.10","properties":[{"key":"EntryName","value":"Urease, subunit C, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00220_B","properties":[{"key":"EntryName","value":"PyrC_classI_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006680","properties":[{"key":"EntryName","value":"Amidohydro-rel"}]},{"database":"InterPro","id":"IPR004722","properties":[{"key":"EntryName","value":"DHOase"}]},{"database":"InterPro","id":"IPR050138","properties":[{"key":"EntryName","value":"DHOase/Allantoinase_Hydrolase"}]},{"database":"InterPro","id":"IPR002195","properties":[{"key":"EntryName","value":"Dihydroorotase_CS"}]},{"database":"InterPro","id":"IPR011059","properties":[{"key":"EntryName","value":"Metal-dep_hydrolase_composite"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"database":"NCBIfam","id":"NF006837","properties":[{"key":"EntryName","value":"PRK09357.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00857","properties":[{"key":"EntryName","value":"pyrC_multi"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43668","properties":[{"key":"EntryName","value":"ALLANTOINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43668:SF2","properties":[{"key":"EntryName","value":"ALLANTOINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01979","properties":[{"key":"EntryName","value":"Amidohydro_1"},{"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":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00483","properties":[{"key":"EntryName","value":"DIHYDROOROTASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAILLKNGLVYQEGEFIKEDVLISGSKIQAIGLDLPEEGAEVYDLKGKLLAPGLVDIHEHYREPGFTYKETIKTGSEAASRGGFTTVCTMPNVDPIPDDLETFEKQVALNEANSCVHLKQYGAITEDLTSDKVVDMAALKEAGAFAFSNDGHGIQQAGTMYEAMQEAAKVGLAICEHIQDDSLYHHGVMNAGKKAEELGLPGILGVSESAQLARDLVLAQATGVHYHACHVSTKESVELIRIAKEYGINVTAEATPHHLLLSEEEIDGNNGYYKMNPPLRSKEDQFALIEGMLDGTIDLIATDHAPHSREEKAGDMRKAAFGIIGNETAFACLYTKFVKSGQMDLSLLLDLMSYQPAKLFGLDAGVLAPGKEADLAVFDLDHAEKLSEEDYLSKGVNTPFTGQEVYGMTALTFVSGKLVYKSKHFAD","length":427,"molWeight":46319,"crc64":"1AB5BC6163C57E30","md5":"61197606E42173C59FD234E62861C095"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":12},"uniParcId":"UPI0000132C67"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q48734","uniProtkbId":"HSLV_LACLE","entryAudit":{"firstPublicDate":"2000-12-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-01-23","entryVersion":98,"sequenceVersion":3},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}],"value":"ATP-dependent protease subunit HslV"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}],"value":"3.4.25.2"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}],"value":"hslV"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}],"value":"Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP-dependent cleavage of peptide bonds with broad specificity.","ecNumber":"3.4.25.2","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}],"value":"Allosterically activated by HslU binding"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}],"value":"A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}],"value":"Belongs to the peptidase T1B family. HslV subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"ATP-dependent protease subunit HslV","featureId":"PRO_0000148115"},{"type":"Active site","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}]},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29101"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}],"ligand":{"name":"Na(+)","id":"ChEBI:CHEBI:29101"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29101"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}],"ligand":{"name":"Na(+)","id":"ChEBI:CHEBI:29101"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29101"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00248"}],"ligand":{"name":"Na(+)","id":"ChEBI:CHEBI:29101"}}],"keywords":[{"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0645","category":"Molecular function","name":"Protease"},{"id":"KW-0915","category":"Ligand","name":"Sodium"},{"id":"KW-0888","category":"Molecular function","name":"Threonine protease"}],"references":[{"referenceNumber":1,"citation":{"id":"8867465","citationType":"journal article","authors":["Becker J.","Brendel M."],"citationCrossReferences":[{"database":"PubMed","id":"8867465"},{"database":"DOI","id":"10.1007/s002849900042"}],"title":"Molecular characterization of the xerC gene of Lactobacillus leichmannii encoding a site-specific recombinase and two adjacent heat shock genes.","publicationDate":"1996","journal":"Curr. Microbiol.","firstPage":"232","lastPage":"236","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 4797 / DSM 20076 / BCRC 10699 / JCM 1148 / NBRC 3073 / NCIMB 7854 / 326 / F59","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X84261","properties":[{"key":"ProteinId","value":"CAA59019.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_013439704.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000053.1"}]},{"database":"AlphaFoldDB","id":"Q48734","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q48734","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009376","properties":[{"key":"GoTerm","value":"C:HslUV protease complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005839","properties":[{"key":"GoTerm","value":"C:proteasome core complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004298","properties":[{"key":"GoTerm","value":"F:threonine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0030163","properties":[{"key":"GoTerm","value":"P:protein catabolic process"},{"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":"cd01913","properties":[{"key":"EntryName","value":"protease_HslV"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.20.10","properties":[{"key":"EntryName","value":"Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00248","properties":[{"key":"EntryName","value":"HslV"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022281","properties":[{"key":"EntryName","value":"ATP-dep_Prtase_HsIV_su"}]},{"database":"InterPro","id":"IPR029055","properties":[{"key":"EntryName","value":"Ntn_hydrolases_N"}]},{"database":"InterPro","id":"IPR001353","properties":[{"key":"EntryName","value":"Proteasome_sua/b"}]},{"database":"InterPro","id":"IPR023333","properties":[{"key":"EntryName","value":"Proteasome_suB-type"}]},{"database":"NCBIfam","id":"TIGR03692","properties":[{"key":"EntryName","value":"ATP_dep_HslV"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003964","properties":[{"key":"EntryName","value":"hslV"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32194:SF0","properties":[{"key":"EntryName","value":"ATP-DEPENDENT PROTEASE SUBUNIT HSLV"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32194","properties":[{"key":"EntryName","value":"METALLOPROTEASE TLDD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00227","properties":[{"key":"EntryName","value":"Proteasome"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56235","properties":[{"key":"EntryName","value":"N-terminal nucleophile aminohydrolases (Ntn hydrolases)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51476","properties":[{"key":"EntryName","value":"PROTEASOME_BETA_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTTICSVKYNGQTAIAGDGQVTLGKSIIAKTTAKKIRRIYHDQVVIGFAGGVADAVSLQEMLEGKLESYSGDLRRAAVEMAQSWRKDQTLQKLEAMVIAFNDQDLLLISGNGEVLEPDESVVAIGSGGYYAQAAAVGMLRHASGMTASEIAKEAVNIAADIDVFTDHEIVTDEIEEK","length":177,"molWeight":18936,"crc64":"842F7277CDEB1305","md5":"691ADC3A89AD85CE975F707C0DE81140"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Active site":1,"Binding site":3},"uniParcId":"UPI000016F8CA"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q48735","uniProtkbId":"HSLU_LACLE","entryAudit":{"firstPublicDate":"2000-12-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2000-12-01","entryVersion":114,"sequenceVersion":2},"annotationScore":2.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"value":"ATP-dependent protease ATPase subunit HslU"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"value":"Unfoldase HslU"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"value":"hslU"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"value":"ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"value":"A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"value":"Belongs to the ClpX chaperone family. HslU subfamily"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"CAA59020.1","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":464,"modifier":"EXACT"}},"description":"ATP-dependent protease ATPase subunit HslU","featureId":"PRO_0000160513"},{"type":"Binding site","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":414,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00249"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"8867465","citationType":"journal article","authors":["Becker J.","Brendel M."],"citationCrossReferences":[{"database":"PubMed","id":"8867465"},{"database":"DOI","id":"10.1007/s002849900042"}],"title":"Molecular characterization of the xerC gene of Lactobacillus leichmannii encoding a site-specific recombinase and two adjacent heat shock genes.","publicationDate":"1996","journal":"Curr. Microbiol.","firstPage":"232","lastPage":"236","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 4797 / DSM 20076 / BCRC 10699 / JCM 1148 / NBRC 3073 / NCIMB 7854 / 326 / F59","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X84261","properties":[{"key":"ProteinId","value":"CAA59020.1"},{"key":"Status","value":"ALT_FRAME"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q48735","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q48735","properties":[{"key":"Description","value":"-"}]},{"database":"MEROPS","id":"X20.005","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009376","properties":[{"key":"GoTerm","value":"C:HslUV protease complex"},{"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:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008233","properties":[{"key":"GoTerm","value":"F:peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0036402","properties":[{"key":"GoTerm","value":"F:proteasome-activating activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043335","properties":[{"key":"GoTerm","value":"P:protein unfolding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"1.10.8.60","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":"2"}]},{"database":"HAMAP","id":"MF_00249","properties":[{"key":"EntryName","value":"HslU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR050052","properties":[{"key":"EntryName","value":"ATP-dep_Clp_protease_ClpX"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR019489","properties":[{"key":"EntryName","value":"Clp_ATPase_C"}]},{"database":"InterPro","id":"IPR004491","properties":[{"key":"EntryName","value":"HslU"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003544","properties":[{"key":"EntryName","value":"hslU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00390","properties":[{"key":"EntryName","value":"hslU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48102","properties":[{"key":"EntryName","value":"ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48102:SF3","properties":[{"key":"EntryName","value":"ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07724","properties":[{"key":"EntryName","value":"AAA_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10431","properties":[{"key":"EntryName","value":"ClpB_D2-small"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01086","properties":[{"key":"EntryName","value":"ClpB_D2-small"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MREKTPKQIVDLLDKYIVGQNEAKKSVAIALYNRYRRAQLPEDVQKDITPKNILMAGPTGVGKTEIARRLADIVDAPFVKVEATKFTEVGYVGRDVESMVRDLANEAVRIVEKEEFVKVEGQAIRQANKTLVRLLVPGVKRNNRQNQMQQMQEMIQSLLAGGGMSEETEEVTDEIRNQRLSVAEKLDRGLLENEEVTIEVEQAPKANPMGDMMGQMGMDMSSMLGDMLPKKKVKRTLPVSQARKLLVQEEEKKLVNYDDIYQKAMDRAGQSGIIFIDEIDKITAADKRNSAGVSREGVQRDILPIVEGSTVSTKYGPLSTDHILFIAAGAFAESKPSDLIPELQGRFPIRVELDALTKDDFVRILKDPQNSLLKQYIALLKADGVDLVFTAEAVDKIAEIAFEVNQGTDNIGARRLATILEKLLEEVLYEGPDMEMGQITITQAYVEQKLSDIVKNKDLTKFIL","length":464,"molWeight":51881,"crc64":"69C6BC9628C1B312","md5":"27F9568DF8CE0652C2896A3D257AADB5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"SEQUENCE CAUTION":1},"countByFeatureType":{"Chain":1,"Binding site":5},"uniParcId":"UPI000012CD1B"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q48733","uniProtkbId":"XERC_LACLE","entryAudit":{"firstPublicDate":"2003-08-22","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":100,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}],"value":"Tyrosine recombinase XerC"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}],"value":"xerC"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}],"value":"Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}],"value":"Forms a cyclic heterotetrameric complex composed of two molecules of XerC and two molecules of XerD"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}],"value":"Belongs to the 'phage' integrase family. XerC subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"Tyrosine recombinase XerC","featureId":"PRO_0000095299"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"Core-binding (CB)","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01248"}]},{"type":"Domain","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"Tyr recombinase","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01246"}]},{"type":"Active site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}]},{"type":"Active site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}]},{"type":"Active site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}]},{"type":"Active site","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}]},{"type":"Active site","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}]},{"type":"Active site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"O-(3'-phospho-DNA)-tyrosine intermediate","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01808"}]}],"keywords":[{"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"id":"KW-0132","category":"Biological process","name":"Cell division"},{"id":"KW-0159","category":"Biological process","name":"Chromosome partition"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0229","category":"Biological process","name":"DNA integration"},{"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"id":"KW-0238","category":"Molecular function","name":"DNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"8867465","citationType":"journal article","authors":["Becker J.","Brendel M."],"citationCrossReferences":[{"database":"PubMed","id":"8867465"},{"database":"DOI","id":"10.1007/s002849900042"}],"title":"Molecular characterization of the xerC gene of Lactobacillus leichmannii encoding a site-specific recombinase and two adjacent heat shock genes.","publicationDate":"1996","journal":"Curr. Microbiol.","firstPage":"232","lastPage":"236","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 4797 / DSM 20076 / BCRC 10699 / JCM 1148 / NBRC 3073 / NCIMB 7854 / 326 / F59","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X84261","properties":[{"key":"ProteinId","value":"CAA59018.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_035184589.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000053.1"}]},{"database":"AlphaFoldDB","id":"Q48733","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q48733","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009037","properties":[{"key":"GoTerm","value":"F:tyrosine-based site-specific recombinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0007059","properties":[{"key":"GoTerm","value":"P:chromosome segregation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006313","properties":[{"key":"GoTerm","value":"P:DNA transposition"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00798","properties":[{"key":"EntryName","value":"INT_XerDC_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.130","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.443.10","properties":[{"key":"EntryName","value":"Intergrase catalytic core"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01808","properties":[{"key":"EntryName","value":"Recomb_XerC_XerD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR044068","properties":[{"key":"EntryName","value":"CB"}]},{"database":"InterPro","id":"IPR011010","properties":[{"key":"EntryName","value":"DNA_brk_join_enz"}]},{"database":"InterPro","id":"IPR013762","properties":[{"key":"EntryName","value":"Integrase-like_cat_sf"}]},{"database":"InterPro","id":"IPR002104","properties":[{"key":"EntryName","value":"Integrase_catalytic"}]},{"database":"InterPro","id":"IPR010998","properties":[{"key":"EntryName","value":"Integrase_recombinase_N"}]},{"database":"InterPro","id":"IPR004107","properties":[{"key":"EntryName","value":"Integrase_SAM-like_N"}]},{"database":"InterPro","id":"IPR011931","properties":[{"key":"EntryName","value":"Recomb_XerC"}]},{"database":"InterPro","id":"IPR023009","properties":[{"key":"EntryName","value":"Tyrosine_recombinase_XerC/XerD"}]},{"database":"InterPro","id":"IPR050090","properties":[{"key":"EntryName","value":"XerCD-like"}]},{"database":"NCBIfam","id":"NF040815","properties":[{"key":"EntryName","value":"recomb_XerA_Arch"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02224","properties":[{"key":"EntryName","value":"recomb_XerC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30349","properties":[{"key":"EntryName","value":"PHAGE INTEGRASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30349:SF77","properties":[{"key":"EntryName","value":"TYROSINE RECOMBINASE XERC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02899","properties":[{"key":"EntryName","value":"Phage_int_SAM_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00589","properties":[{"key":"EntryName","value":"Phage_integrase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56349","properties":[{"key":"EntryName","value":"DNA breaking-rejoining enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51900","properties":[{"key":"EntryName","value":"CB"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51898","properties":[{"key":"EntryName","value":"TYR_RECOMBINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTLEEQFLSYLKNERSYSPKTVLAYQKDLAAAKKFWQENGGFPGWDQISRRDLEIYLLATGQKLASSTLSRKLSSLKSFYRLLTRRGLVKADPTVAIQLRRGKKKLPEFFYQDEVGQVIRSLNDGKPLTVRNRAIVALFYATGMRLSELTDLKIKQLDLENGMILVHGKGNKDRYVFFDQESKKYLEEYLQVARPSLLKNEPDTEAVFLNKLGRPISSRGIAKAVQQIFQKAGLTAGAHPHELRHSFATAMLNNGADLRSVQELLGHEDLSTTQIYTHVSMQHLTAEYRQHFPRK","length":295,"molWeight":33719,"crc64":"EAEA676E187F5042","md5":"8DF7E794052B8B7F19FAA6B140F37750"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":2,"Active site":6},"uniParcId":"UPI00000B1313"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XUW1","uniProtkbId":"A0ABT1XUW1_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970422.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"value":"Dihydroorotate dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"value":"DHOD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"value":"DHODase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"value":"DHOdehase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"value":"1.3.-.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"value":"pyrD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970422.1"}],"value":"DS743_00770"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002934"}],"value":"Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049578"}],"value":"Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-dihydroorotate + A = orotate + AH2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18073"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:17499"},{"database":"ChEBI","id":"CHEBI:30839"},{"database":"ChEBI","id":"CHEBI:30864"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-dihydroorotate + fumarate = orotate + succinate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30059"},{"database":"ChEBI","id":"CHEBI:29806"},{"database":"ChEBI","id":"CHEBI:30031"},{"database":"ChEBI","id":"CHEBI:30839"},{"database":"ChEBI","id":"CHEBI:30864"}],"ecNumber":"1.3.98.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001694"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5,6-dihydrothymine + NAD(+) = thymine + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28791"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17821"},{"database":"ChEBI","id":"CHEBI:27468"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.3.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047685"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5,6-dihydrouracil + NAD(+) = uracil + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20189"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15901"},{"database":"ChEBI","id":"CHEBI:17568"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.3.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048792"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"value":"Binds 1 FMN per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004725"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049714"}],"value":"Heterotetramer of 2 PreA and 2 PreT subunits"}],"commentType":"SUBUNIT"},{"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":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008008"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"value":"Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970422.1"}],"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":7,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"Dihydroorotate dehydrogenase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01180"}]},{"type":"Active site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}]},{"type":"Binding site","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00224"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970422.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970422.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000015","properties":[{"key":"ProteinId","value":"MCR5970422.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003615650.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000015.1"}]},{"database":"Proteomes","id":"UP001524940","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:1990663","properties":[{"key":"GoTerm","value":"F:dihydroorotate dehydrogenase (fumarate) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004159","properties":[{"key":"GoTerm","value":"F:dihydropyrimidine dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0002058","properties":[{"key":"GoTerm","value":"F:uracil binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"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-UniRule"}]},{"database":"GO","id":"GO:0006210","properties":[{"key":"GoTerm","value":"P:thymine catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006212","properties":[{"key":"GoTerm","value":"P:uracil catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04740","properties":[{"key":"EntryName","value":"DHOD_1B_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000027","properties":[{"key":"EntryName","value":"Dihydropyrimidine dehydrogenase [NADP(+)]"},{"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_00224","properties":[{"key":"EntryName","value":"DHO_dh_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR033888","properties":[{"key":"EntryName","value":"DHOD_1B"}]},{"database":"InterPro","id":"IPR024920","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_1"}]},{"database":"InterPro","id":"IPR012135","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_1_2"}]},{"database":"InterPro","id":"IPR005720","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_cat"}]},{"database":"InterPro","id":"IPR001295","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_CS"}]},{"database":"InterPro","id":"IPR049622","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_I"}]},{"database":"NCBIfam","id":"NF005574","properties":[{"key":"EntryName","value":"PRK07259.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01037","properties":[{"key":"EntryName","value":"pyrD_sub1_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43073","properties":[{"key":"EntryName","value":"DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43073:SF2","properties":[{"key":"EntryName","value":"DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01180","properties":[{"key":"EntryName","value":"DHO_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000164","properties":[{"key":"EntryName","value":"DHO_oxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51395","properties":[{"key":"EntryName","value":"FMN-linked oxidoreductases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00912","properties":[{"key":"EntryName","value":"DHODEHASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAEVNLAVELPGLKLKNPVMPASGTFAFGDLPENFNWDEMGAIVLKTATRHARTGNPQPQISLLADGVMNAVGLTNPGAEVVASEKIPALREKHPDLPILASVGGESVEDYVEVAEILAAAKPDALELNLSCPNVSEGGMTFGIVPEMVEKITRLVKEKVDLPVYVKLTPNVTSIVEIAQAAERGGADGLTLINTLLGLHLDLKTRRPVLGNDFGGLSGQAVKPVAVRMVAQVRQATSLPIIGVGGINSPEDAAEFILAGASAVQIGSMAFHDKLAIKHVIDGLPAVLADMGASDVTSLVGQWQSNKQ","length":309,"molWeight":32340,"crc64":"EE370219B2AACCFD","md5":"C15FC7677A0CC7FD7AF2E71762B39460"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":12},"uniParcId":"UPI000202DA48"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XVR0","uniProtkbId":"A0ABT1XVR0_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970722.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"Endonuclease MutS2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"3.1.-.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"Ribosome-associated protein quality control-upstream factor"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"RQC-upstream factor"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"RqcU"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"3.6.4.-"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"mutS2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"rqcU"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970722.1"}],"value":"DS743_02410"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"Acts as a ribosome collision sensor, splitting the ribosome into its 2 subunits. Detects stalled/collided 70S ribosomes which it binds and splits by an ATP-hydrolysis driven conformational change. Acts upstream of the ribosome quality control system (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes and their subsequent degradation. Probably generates substrates for RQC"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"Endonuclease that is involved in the suppression of homologous recombination and thus may have a key role in the control of bacterial genetic diversity"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"Homodimer. Binds to stalled ribosomes, contacting rRNA"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"value":"Belongs to the DNA mismatch repair MutS family. MutS2 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970722.1"}],"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":712,"modifier":"EXACT"},"end":{"value":787,"modifier":"EXACT"}},"description":"Smr","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50828"}]},{"type":"Region","location":{"start":{"value":688,"modifier":"EXACT"},"end":{"value":712,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Coiled coil","location":{"start":{"value":524,"modifier":"EXACT"},"end":{"value":638,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Compositional bias","location":{"start":{"value":688,"modifier":"EXACT"},"end":{"value":709,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022759"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"id":"KW-0255","category":"Molecular function","name":"Endonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022730"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00092"}],"id":"KW-0699","category":"Molecular function","name":"rRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970722.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970722.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000022","properties":[{"key":"ProteinId","value":"MCR5970722.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP001524940","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"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:0140664","properties":[{"key":"GoTerm","value":"F:ATP-dependent DNA damage sensor activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004519","properties":[{"key":"GoTerm","value":"F:endonuclease activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030983","properties":[{"key":"GoTerm","value":"F:mismatched DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043023","properties":[{"key":"GoTerm","value":"F:ribosomal large subunit binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006298","properties":[{"key":"GoTerm","value":"P:mismatch repair"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0045910","properties":[{"key":"GoTerm","value":"P:negative regulation of DNA recombination"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0072344","properties":[{"key":"GoTerm","value":"P:rescue of stalled cytosolic ribosome"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd03280","properties":[{"key":"EntryName","value":"ABC_MutS2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000830","properties":[{"key":"EntryName","value":"Endonuclease MutS2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1370.110","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_00092","properties":[{"key":"EntryName","value":"MutS2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000432","properties":[{"key":"EntryName","value":"DNA_mismatch_repair_MutS_C"}]},{"database":"InterPro","id":"IPR007696","properties":[{"key":"EntryName","value":"DNA_mismatch_repair_MutS_core"}]},{"database":"InterPro","id":"IPR036187","properties":[{"key":"EntryName","value":"DNA_mismatch_repair_MutS_sf"}]},{"database":"InterPro","id":"IPR046893","properties":[{"key":"EntryName","value":"MSSS"}]},{"database":"InterPro","id":"IPR045076","properties":[{"key":"EntryName","value":"MutS"}]},{"database":"InterPro","id":"IPR005747","properties":[{"key":"EntryName","value":"MutS2"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR002625","properties":[{"key":"EntryName","value":"Smr_dom"}]},{"database":"InterPro","id":"IPR036063","properties":[{"key":"EntryName","value":"Smr_dom_sf"}]},{"database":"NCBIfam","id":"TIGR01069","properties":[{"key":"EntryName","value":"mutS2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48466:SF2","properties":[{"key":"EntryName","value":"OS10G0509000 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48466","properties":[{"key":"EntryName","value":"OS10G0509000 PROTEIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20297","properties":[{"key":"EntryName","value":"MSSS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00488","properties":[{"key":"EntryName","value":"MutS_V"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01713","properties":[{"key":"EntryName","value":"Smr"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005814","properties":[{"key":"EntryName","value":"MutS_YshD"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00534","properties":[{"key":"EntryName","value":"MUTSac"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00533","properties":[{"key":"EntryName","value":"MUTSd"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00463","properties":[{"key":"EntryName","value":"SMR"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48334","properties":[{"key":"EntryName","value":"DNA repair protein MutS, domain III"},{"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":"SSF160443","properties":[{"key":"EntryName","value":"SMR domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00486","properties":[{"key":"EntryName","value":"DNA_MISMATCH_REPAIR_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50828","properties":[{"key":"EntryName","value":"SMR"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MMNHKILDILEYQEISSRLAEQAVTAPAKSKALNLQPASDRETVSRALSETKALVDLDRIKGQLPLTDFQDVAPSLKRLKVKADLNALELGNILLIFTLAQESSRFVEDAEENKTLDLAAIETLLDDLELPDDLYRRLRTSLTYDGEVLDTASADLARLRHGRLATEAEIKEKMTAYTKGKNGQYLSEQIVTIRDDRYVIPVKQEYRYKFGGVVHDQSASGQTLFVEPAAILPLNNRLQNLLAEERQEIHRVLHELSLDAREEMEAIKRVAAALSELDFLQAKAKLAKQMRASQPALSADQSFKLLGARHPLIDPDKVVANDIALGQDFDTILITGPNTGGKTITLKTAGLLQLMAQSGLFIPANEGSSVAVFDQIFADIGDEQSIEQSLSTFSSHINDIVAIMKRVSDQSLVLIDEIGAGTDPEEGARLAISILDFFRKKGAKIIVTTHYPELKLYGYNRERTTNASMEFDIKTLSPTYRLQMGIPGHSNAFAIARRLGMREDVVAGAEKLMSSDDSDINHMIDELNKQTKLVTENKQKLQTSLDRAKQLEKKLQDALDIYNQRVQKQLDFALDQANEIVAKKRKKADKIIAELEEARKEGMQVKTNQLMDAKGEFNQLAKQEANLAKNKVLQKEKKRHHVQVGDKVKVLSYGQTGTVTKQLGEHDYEVSLGRIKLKVTDRDIDKLAAGQKQQAQRRATSASRSSRARSSLDLRGQRYEEAMVNLDRYFDTILLSGLSTVTIIHGIGTGAIRQGVQQYLKRNKHVKTYSYAPANEGGTGATIVTLK","length":787,"molWeight":87672,"crc64":"0C254BB6BC654275","md5":"86AAAFB6B96B29CC9D1BA6A7E7B50439"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Coiled coil":2,"Compositional bias":1,"Binding site":1},"uniParcId":"UPI001142D52C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XX76","uniProtkbId":"A0ABT1XX76_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971237.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bifunctional protein GlmU"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"UDP-N-acetylglucosamine pyrophosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.7.7.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"N-acetylglucosamine-1-phosphate uridyltransferase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Glucosamine-1-phosphate N-acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.3.1.157"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971237.1"}],"value":"DS743_05315"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005166"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005208"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971237.1"}],"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":219,"modifier":"EXACT"}},"description":"Nucleotidyl transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00483"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":461,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":350,"modifier":"EXACT"},"end":{"value":350,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":422,"modifier":"EXACT"},"end":{"value":422,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"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":"HAMAP-Rule","id":"MF_01631"}],"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_01631"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971237.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971237.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000044","properties":[{"key":"ProteinId","value":"MCR5971237.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_002878710.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000044.1"}]},{"database":"GeneID","id":"69668383","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001524940","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:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR018357","properties":[{"key":"EntryName","value":"Hexapep_transf_CS"}]},{"database":"InterPro","id":"IPR005835","properties":[{"key":"EntryName","value":"NTP_transferase_dom"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"NF010934","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00483","properties":[{"key":"EntryName","value":"NTP_transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00101","properties":[{"key":"EntryName","value":"HEXAPEP_TRANSFERASES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGKYVVVLAAGKGTRMKSKLYKVLHQVCGKAMVEHVVDAARAVKPSKIVTIVGHGAEDVEKVLAGKSEFAMQEEQLGTGHAVMQAEGQLAALEGATLVVTGDTPLFTSETFEKLFAYHEEEGNAATVLTAEAPDPFGYGRIIRDDQGNVLRIVEQKDGKPEELKVKEINTGVFCFDNQDLWAALKQVGNDNSQGEYYLTDVLEILRKAGKKVGAYKMPDFSESLGVNDRIALAEATRIMQRRINEGHMRDGVTFIDPATAYIDADVEIGNDTVIEGGVTIKGHTVIGSDCLITSGSRIVDSQIGNGVTVTSSTIEESIMEDNTDIGPNSHLRPKALIKRGAHLGNFVEVKKAEIGENTKVGHLTYVGDATLGKDINVGCGVIFSNFDGVKKFHTTVGDKSFIGAGSTLVSPINVADHAFIAADSTITKDVGKYEMAIARGRQVNKEDYWHKLPLSEDEEWK","length":461,"molWeight":49870,"crc64":"2281E22FDAD1B414","md5":"D40D3D305303B9D9039435609E0663C4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":3,"Active site":1,"Binding site":16},"uniParcId":"UPI0001EC2F15"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XY42","uniProtkbId":"A0ABT1XY42_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971554.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphohexokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971554.1"}],"value":"pfkA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971554.1"}],"value":"DS743_07020"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002659"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"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_00339"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"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_00339"}],"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_00339"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971554.1"}],"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":3,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"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_00339"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"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_00339"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971554.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971554.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000046","properties":[{"key":"ProteinId","value":"MCR5971554.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_002877605.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000046.1"}]},{"database":"GeneID","id":"69668804","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001524940","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: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:UniProtKB-UniRule"}]},{"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:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00763","properties":[{"key":"EntryName","value":"Bacterial_PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.450:FF:000001","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":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00339","properties":[{"key":"EntryName","value":"Phosphofructokinase_I_B1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR012003","properties":[{"key":"EntryName","value":"ATP_PFK_prok-type"}]},{"database":"InterPro","id":"IPR012828","properties":[{"key":"EntryName","value":"PFKA_ATP_prok"}]},{"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":"TIGR02482","properties":[{"key":"EntryName","value":"PFKA_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002872","properties":[{"key":"EntryName","value":"PRK03202.1"},{"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":"1"}]},{"database":"PIRSF","id":"PIRSF000532","properties":[{"key":"EntryName","value":"ATP_PFK_prok"},{"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":"1"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKRIGILTSGGDAPGMNAAVRAVTRVAIANGLEVFGIRYGFAGLVAGDIFPLESEDVAHLINVSGTFLYSARYPEFAEEEGQLAGIEQLKKHGIDAVVVIGGDGSYHGALQLTRHGFNSIGLPGTIDNDIPYTDATIGYDTACMTAMDAIDKIRDTASSHHRVFIVNVMGRNCGDIAMRVGVACGADAIVIPERPYDVEEIANRLKQAQESGKDHGVVVVAEGVMTADQFMAELKKHGDFDVRANVLGHMQRGGTPTVSDRVLASKLGSEAVHLLLEGKGGLAVGIENGKVTSHDILDLFDESHKGDYDLLKLNADLSR","length":319,"molWeight":33940,"crc64":"8B60B05EE89CC716","md5":"6DCC9718A197321716F4F17696A2D679"},"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":14},"uniParcId":"UPI0001EC309A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XY64","uniProtkbId":"A0ABT1XY64_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971577.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971577.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971577.1"}],"value":"DS743_07135"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19397"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"6.3.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (R)-4'-phosphopantetheine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16793"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"4.1.1.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Binds 1 FMN per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the C-terminal section; belongs to the PPC synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971577.1"}],"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":3,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"DNA/pantothenate metabolism flavoprotein C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04127"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971577.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971577.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000046","properties":[{"key":"ProteinId","value":"MCR5971577.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_141372436.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000046.1"}]},{"database":"Proteomes","id":"UP001524940","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0071513","properties":[{"key":"GoTerm","value":"C:phosphopantothenoylcysteine decarboxylase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004632","properties":[{"key":"GoTerm","value":"F:phosphopantothenate--cysteine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004633","properties":[{"key":"GoTerm","value":"F:phosphopantothenoylcysteine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015941","properties":[{"key":"GoTerm","value":"P:pantothenate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.10300","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1950","properties":[{"key":"EntryName","value":"Flavin prenyltransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02225","properties":[{"key":"EntryName","value":"CoaBC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR035929","properties":[{"key":"EntryName","value":"CoaB-like_sf"}]},{"database":"InterPro","id":"IPR005252","properties":[{"key":"EntryName","value":"CoaBC"}]},{"database":"InterPro","id":"IPR007085","properties":[{"key":"EntryName","value":"DNA/pantothenate-metab_flavo_C"}]},{"database":"InterPro","id":"IPR036551","properties":[{"key":"EntryName","value":"Flavin_trans-like"}]},{"database":"InterPro","id":"IPR003382","properties":[{"key":"EntryName","value":"Flavoprotein"}]},{"database":"NCBIfam","id":"TIGR00521","properties":[{"key":"EntryName","value":"coaBC_dfp"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359","properties":[{"key":"EntryName","value":"HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359:SF6","properties":[{"key":"EntryName","value":"PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04127","properties":[{"key":"EntryName","value":"DFP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02441","properties":[{"key":"EntryName","value":"Flavoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102645","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52507","properties":[{"key":"EntryName","value":"Homo-oligomeric flavin-containing Cys decarboxylases, HFCD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MARISVYMTGGIAAYKAVSVVRGLQKAGHEVRVAMTAKSERFVGPATLAALTKWPVLDDLFSPGRQAEIAHIDLADWSQLALVVPADANILAKLAQGIGDDAVSTTLLALHCPRLIVPAMNSHMWENPAVQRNLRLLKEGGDRIMEPAVGRLAEGYAGKGRMPEAEEILAWVNDQLDLPAKGKRIVVTAGGNLEAIDPVRFIGNRSSGKMGFRLAEAAAKRGAEVDLIYGNVSVSLPRDARIHLHPALLSAQAMLEKLEELFPAADALLMAAAVSDWRPKEAADHKLKKQAGVEEMTLQLVKNPDLLKTMAQKKRPDQVVIGFAAETNDLLANASRKLAEKGADLIVANDVSGDAFGGDEDQVTILEQGKELDPWPRMSKQAVADRLIELTLARLAEKKNKKK","length":403,"molWeight":43563,"crc64":"667CB4AE864E1F0A","md5":"65CDE037A5081D214DC06783E5F54E02"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":6},"uniParcId":"UPI001141822E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XYJ6","uniProtkbId":"A0ABT1XYJ6_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971703.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthetase ammonia chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971703.1"}],"value":"DS743_07890"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"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":"HAMAP-Rule","id":"MF_01210"}]}},{"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"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Binds 4 Mg(2+) or Mn(2+) ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971703.1"}],"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":133,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":672,"modifier":"EXACT"},"end":{"value":864,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":933,"modifier":"EXACT"},"end":{"value":1066,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":933,"modifier":"EXACT"},"end":{"value":1066,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":708,"modifier":"EXACT"},"end":{"value":708,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":749,"modifier":"EXACT"},"end":{"value":749,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":751,"modifier":"EXACT"},"end":{"value":751,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":755,"modifier":"EXACT"},"end":{"value":755,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":780,"modifier":"EXACT"},"end":{"value":780,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":781,"modifier":"EXACT"},"end":{"value":781,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":782,"modifier":"EXACT"},"end":{"value":782,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":783,"modifier":"EXACT"},"end":{"value":783,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":823,"modifier":"EXACT"},"end":{"value":823,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":823,"modifier":"EXACT"},"end":{"value":823,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":823,"modifier":"EXACT"},"end":{"value":823,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"3"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"4"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"3"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}},{"type":"Binding site","location":{"start":{"value":837,"modifier":"EXACT"},"end":{"value":837,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"4"}},{"type":"Binding site","location":{"start":{"value":837,"modifier":"EXACT"},"end":{"value":837,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971703.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971703.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000052","properties":[{"key":"ProteinId","value":"MCR5971703.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_035184468.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000052.1"}]},{"database":"Proteomes","id":"UP001524940","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: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-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"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-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","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":"3.30.470.20:FF:000026","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"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":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"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":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"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":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"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":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01209","properties":[{"key":"EntryName","value":"GARS_A"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"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":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"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":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKRDDIKKVLVIGSGPIIIGQAAEFDYAGTQACRALREEGIEVVLINSNPATIMTDGDMADHVYIEPLTVPVVKQLMEKEKPDALLPTMGGQNALNIAMALADEGFLEKHHVKTIGTDTDTIKMAEDRLEFKNLMERIGEPVAKSVVVNYVEDAIAFAKEIGYPVVVRPAYTLGGTGGGIAHNEQELHEICSNGLRLSRVTECLIEQSIAGWKEVEYEVMRDGAGNCITVCNMENMDPVGVHTGDSIVVAPSQTLSDKDYQMLRSSALNIITALNIKGGCNVQFALNPDSFEYCVIEVNPRVSRSSALASKATGYPIAKLATKIALGYNLDEIVNAVTGKTYASYEPTLDYIVCKIPKWPFDKFYDASRKLGTQMKATGEVMAICNNFEGAFMKALRSLEQDSYYLYNEEIAQLSADNLRKDLRKIDDKRAFRIAEALRKGVSIREIHAITKIDVWFIDKIKHLVEIEDRLKSEELTPDLLKLAKHCEFPDRVIASLTGKTADEVYYLRKGLKITAAFKTVDTCAAEFDAETPYFYSVYGGEHEIQPDRSKKKVIVFGSGPIRIGQGIEFDYCCVHSVWALKEAGYETIIVNNNPETVSTDFDIADRLYFEPLTAEDVQSIIELEQPDGAIVQFGGQTAIKLSQDLMKMGVPILGTSADSVDAAEDRERFDEILEKCQIDRPKGQTVFTAEEALKAANELGYPVLVRPSYVLGGAGMEIALNDGDLKRFIDHITSQFNIEDHPILIDKYLAGKECEVDAICDDEGILIPGIMEHVERAGVHSGDSISIYPPQKISQEMKERIVEYSKRLAKALRVKGLMNIQFIVYENKVYVIEVNPRSSRTIPYISKVTGIPLVDVATNVIIGKSIKEQGYDYGLAPEKKTVAVKMPVFSFEKITGAEIALGPEMKSTGEVLGISEDVEEAMYKAFMGTGLDLPKHKKVICTVKDSAKEEFLPIAKEYHNFGYDLYATQGTYDFLQSHGIPARLVNRINDKENTIFDLILTETVDLVIDIPTRNNNLKDGFLIRRFAVEAGVPIYTSLDTARALIHALEAKHDNKISLVDITKL","length":1066,"molWeight":118244,"crc64":"2B38882F27A00500","md5":"1EAF2C33E6F09561C934CAFE23E0B2CC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":2,"Binding site":38},"uniParcId":"UPI0004AC3C4E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1Y005","uniProtkbId":"A0ABT1Y005_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971848.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Multifunctional fusion protein"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"GTP cyclohydrolase-2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"3.5.4.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"GTP cyclohydrolase II"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"3,4-dihydroxy-2-butanone 4-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"DHBP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"4.1.99.12"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"ribB"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"ribA"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971848.1"}],"value":"DS743_08745"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002284"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18457"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:58121"},{"database":"ChEBI","id":"CHEBI:58830"}],"ecNumber":"4.1.99.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 2 phosphate + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23704"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58614"}],"ecNumber":"3.5.4.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049295"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Binds 2 divalent metal cations per subunit. Magnesium or manganese."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004904"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004853"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"Belongs to the GTP cyclohydrolase II family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005520"}],"value":"In the N-terminal section; belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971848.1"}],"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":365,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00925"}]},{"type":"Active site","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}]},{"type":"Active site","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}]},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Essential for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}]},{"type":"Site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"Essential for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022619"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0686","category":"Biological process","name":"Riboflavin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971848.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971848.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000055","properties":[{"key":"ProteinId","value":"MCR5971848.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_035185728.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000055.1"}]},{"database":"Proteomes","id":"UP001524940","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:0008686","properties":[{"key":"GoTerm","value":"F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003935","properties":[{"key":"GoTerm","value":"F:GTP cyclohydrolase II activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00641","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10990:FF:000002","properties":[{"key":"EntryName","value":"GTP cyclohydrolase-2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.870.10:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.870.10","properties":[{"key":"EntryName","value":"DHBP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10990","properties":[{"key":"EntryName","value":"GTP cyclohydrolase II"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00179","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00180","properties":[{"key":"EntryName","value":"RibB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017945","properties":[{"key":"EntryName","value":"DHBP_synth_RibB-like_a/b_dom"}]},{"database":"InterPro","id":"IPR000422","properties":[{"key":"EntryName","value":"DHBP_synthase_RibB"}]},{"database":"InterPro","id":"IPR032677","properties":[{"key":"EntryName","value":"GTP_cyclohydro_II"}]},{"database":"InterPro","id":"IPR000926","properties":[{"key":"EntryName","value":"RibA"}]},{"database":"InterPro","id":"IPR036144","properties":[{"key":"EntryName","value":"RibA-like_sf"}]},{"database":"NCBIfam","id":"NF001591","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00505","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00506","properties":[{"key":"EntryName","value":"ribB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327:SF18","properties":[{"key":"EntryName","value":"3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE II-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00926","properties":[{"key":"EntryName","value":"DHBP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00925","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001259","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF142695","properties":[{"key":"EntryName","value":"RibA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55821","properties":[{"key":"EntryName","value":"YrdC/RibB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDVKKIQDAIAWMKQGGLVIVADDEDREAEGDMIGLGSKVTPEKINFMTKHARGLLCTSIGREIAERLELPQMWQDNTDPFGTAFTVSVDYKTTTTGISAYDRATTIKALADPEAKPEAFFKPGHCFPLVAKDGGVLERNGHTEASVTLARLAGEAEVAYICEILKEDGHMARRPELEEIAKEYDLPYFTIAELQEYCQSFASSRSEFVKLPTDYGDFEIKDYGNGNLVIKKGEIAKNEPVMLRIHSKCLTGDVFGSKRCDCGHQLHQAMRRIEEKGSGLILYLNQEGRGIGLTNKLRAYALQDQGHDTYDANLLLGFAPDERKYDVAAKMIKDLGIKQVQLLTNNPDKIKQLEEAGVEITDRLPLEIAATAEDRRYLETKRDRFKHMLVSL","length":392,"molWeight":43867,"crc64":"CB23155BFBD2053E","md5":"51D977BAAE66AA298D7BDC11D4B974E0"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":3,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":15,"Site":2},"uniParcId":"UPI0004AC3DF0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1Y0L6","uniProtkbId":"A0ABT1Y0L6_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971243.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"6.3.4.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine 5'-triphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine triphosphate synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"UTP--ammonia ligase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"pyrG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971243.1"}],"value":"DS743_05345"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"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"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971243.1"}],"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":3,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":528,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":510,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":512,"modifier":"EXACT"},"end":{"value":512,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":356,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":465,"modifier":"EXACT"},"end":{"value":465,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971243.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5971243.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000044","properties":[{"key":"ProteinId","value":"MCR5971243.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_002878695.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000044.1"}]},{"database":"GeneID","id":"69668389","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001524940","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","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_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"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":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKYIFVTGGVVSSLGKGITASSIGRLLKNRGLKVTMQKFDPYINIDPGTMNPYQHGEVFVTDDGTEADLDLGHYERLVDVRTSKYSNVTTGKIYQEVLQRERRGDYRGGTVQVIPHVTNMIKEKVMRAAQMTDTDVVISEIGGTVGDMESTPFMEAIRQMRREVGSENVMYVHVTFVPYLRAAKELKSKPTQQSVSMLRSIGIQPNMLVLRSEMPVPQEMKDKISTFTDVPVDYIVESLDAPSLFDVPLSYQEQGVDQKVVDFLHIDSPKPVADMDEWRRMDERAKNLKYKTKITLVGKYVELEDAYISVTDALQHAGYLYNSKIEVEKIQAEDITEDNVAELLKDTQGLIVPGGFGTRGLEGMITSIKYAREHDIPFLGICLGMQMASVEFARNVLHLEDANSAEAEPNCKNNIIDLMADQRDQEKIGGTLRLGLYPAMLKAGTKTRECYDGQEVIQERHRHRYEFNNKYREDFEKAGMTFSGVSPDNHLVEIVEITDKKFFVAAQYHPEFLSRPNRPEGLFKGFIGAASGLQVDKF","length":539,"molWeight":60789,"crc64":"92A1E76909F5BAE2","md5":"0571E6253D999BE69284970ED0848109"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Active site":4,"Binding site":17},"uniParcId":"UPI00032FF870"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XUJ6","uniProtkbId":"A0ABT1XUJ6_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970315.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"value":"Tyrosine--tRNA ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"value":"6.1.1.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"value":"Tyrosyl-tRNA synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"value":"TyrRS"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"value":"tyrS"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970315.1"}],"value":"DS743_00145"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"value":"Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tRNA(Tyr) + L-tyrosine + ATP = L-tyrosyl-tRNA(Tyr) + AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10220"},{"database":"Rhea","id":"RHEA-COMP:9706"},{"database":"Rhea","id":"RHEA-COMP:9707"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58315"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78536"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.1.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048248"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"value":"Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970315.1"}],"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":337,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"Tyrosine--tRNA ligase SYY-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF22421"}]},{"type":"Motif","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"'HIGH' region","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}]},{"type":"Motif","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"'KMSKS' region","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}]},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"ligand":{"name":"L-tyrosine","id":"ChEBI:CHEBI:58315"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"ligand":{"name":"L-tyrosine","id":"ChEBI:CHEBI:58315"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"ligand":{"name":"L-tyrosine","id":"ChEBI:CHEBI:58315"}},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023146"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"id":"KW-0030","category":"Molecular function","name":"Aminoacyl-tRNA synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02006"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00182"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970315.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970315.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000008","properties":[{"key":"ProteinId","value":"MCR5970315.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_002877898.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000008.1"}]},{"database":"GeneID","id":"69668317","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001524940","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:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004831","properties":[{"key":"GoTerm","value":"F:tyrosine-tRNA ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006437","properties":[{"key":"GoTerm","value":"P:tyrosyl-tRNA aminoacylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00165","properties":[{"key":"EntryName","value":"S4"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00805","properties":[{"key":"EntryName","value":"TyrRS_core"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.240.10:FF:000001","properties":[{"key":"EntryName","value":"Tyrosine--tRNA ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.290.10","properties":[{"key":"EntryName","value":"RNA-binding S4 domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.240.10","properties":[{"key":"EntryName","value":"Tyrosyl-Transfer RNA Synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02006","properties":[{"key":"EntryName","value":"Tyr_tRNA_synth_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001412","properties":[{"key":"EntryName","value":"aa-tRNA-synth_I_CS"}]},{"database":"InterPro","id":"IPR002305","properties":[{"key":"EntryName","value":"aa-tRNA-synth_Ic"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"InterPro","id":"IPR036986","properties":[{"key":"EntryName","value":"S4_RNA-bd_sf"}]},{"database":"InterPro","id":"IPR054608","properties":[{"key":"EntryName","value":"SYY-like_C"}]},{"database":"InterPro","id":"IPR002307","properties":[{"key":"EntryName","value":"Tyr-tRNA-ligase"}]},{"database":"InterPro","id":"IPR024088","properties":[{"key":"EntryName","value":"Tyr-tRNA-ligase_bac-type"}]},{"database":"InterPro","id":"IPR024107","properties":[{"key":"EntryName","value":"Tyr-tRNA-ligase_bac_1"}]},{"database":"NCBIfam","id":"TIGR00234","properties":[{"key":"EntryName","value":"tyrS"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11766:SF0","properties":[{"key":"EntryName","value":"TYROSINE--TRNA LIGASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11766","properties":[{"key":"EntryName","value":"TYROSYL-TRNA SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22421","properties":[{"key":"EntryName","value":"SYY_C-terminal"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00579","properties":[{"key":"EntryName","value":"tRNA-synt_1b"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01040","properties":[{"key":"EntryName","value":"TRNASYNTHTYR"}]},{"database":"SUPFAM","id":"SSF55174","properties":[{"key":"EntryName","value":"Alpha-L RNA-binding motif"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00178","properties":[{"key":"EntryName","value":"AA_TRNA_LIGASE_I"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50889","properties":[{"key":"EntryName","value":"S4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MANFDILEDLKWRGAINQETDEEGLRDYLAKHDDLALYCGTDPTGDSLHIGHLIPFMILKRFQLAGYKPVIVIGGGTGSIGDPSGRSTERVLQSEETIKHNEEALTAQMVKLFGTENFRIVNNRDWLGKMTLLEFLRDYGKLFQVNNMLNKEVVASRLENGISFTEFSYQILQAIDFYILNRDHGVQMQIGGADQWGNITAGIDLIHRLEGADRPAFGLTIPLMLKADGTKFGKSAGGAVWLDPEKTSPYEFYQFWINQDDRDVIKYLKYFTFLNHEEIDALEEKVKTEPWKREAQKRLAEEVTKFVHGEEGLKEAQTVTEALFSGNVKDLTTKQVEIALAKAPSAESGAEKKNLVDFLVDTKIESSKRQAREDVNNGAIYVNGDRIQDTDFEVDPAAAFDGKFVIIRKGKKKYTLVHIKG","length":421,"molWeight":47478,"crc64":"D6D32587DB6EAFE7","md5":"3ABF2E34238364B319DF96C8F4DAAF28"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Motif":2,"Binding site":4},"uniParcId":"UPI0001DC94AD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XUM5","uniProtkbId":"A0ABT1XUM5_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970352.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000520"}],"value":"Adenylosuccinate synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"value":"AMPSase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"value":"AdSS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000520"}],"value":"6.3.4.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"value":"IMP--aspartate ligase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"value":"purA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970352.1"}],"value":"DS743_00350"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"IMP + L-aspartate + GTP = N(6)-(1,2-dicarboxyethyl)-AMP + GDP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15753"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57567"},{"database":"ChEBI","id":"CHEBI:58053"},{"database":"ChEBI","id":"CHEBI:58189"}],"ecNumber":"6.3.4.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000520"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000520"}],"value":"Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000520"}],"value":"Belongs to the adenylosuccinate synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970352.1"}],"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":"Active site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}]},{"type":"Active site","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}]},{"type":"Active site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10134"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00011"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970352.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970352.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000011","properties":[{"key":"ProteinId","value":"MCR5970352.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_072544250.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000011.1"}]},{"database":"Proteomes","id":"UP001524940","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:0004019","properties":[{"key":"GoTerm","value":"F:adenylosuccinate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044208","properties":[{"key":"GoTerm","value":"P:'de novo' AMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046040","properties":[{"key":"GoTerm","value":"P:IMP metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03108","properties":[{"key":"EntryName","value":"AdSS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.300.10:FF:000001","properties":[{"key":"EntryName","value":"Adenylosuccinate synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.170.10:FF:000001","properties":[{"key":"EntryName","value":"Adenylosuccinate synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.440.10","properties":[{"key":"EntryName","value":"Adenylosuccinate Synthetase, subunit A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.300.10","properties":[{"key":"EntryName","value":"Adenylosuccinate Synthetase, subunit A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.170.10","properties":[{"key":"EntryName","value":"Adenylosuccinate Synthetase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00011","properties":[{"key":"EntryName","value":"Adenylosucc_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR018220","properties":[{"key":"EntryName","value":"Adenylosuccin_syn_GTP-bd"}]},{"database":"InterPro","id":"IPR033128","properties":[{"key":"EntryName","value":"Adenylosuccin_syn_Lys_AS"}]},{"database":"InterPro","id":"IPR042109","properties":[{"key":"EntryName","value":"Adenylosuccinate_synth_dom1"}]},{"database":"InterPro","id":"IPR042110","properties":[{"key":"EntryName","value":"Adenylosuccinate_synth_dom2"}]},{"database":"InterPro","id":"IPR042111","properties":[{"key":"EntryName","value":"Adenylosuccinate_synth_dom3"}]},{"database":"InterPro","id":"IPR001114","properties":[{"key":"EntryName","value":"Adenylosuccinate_synthetase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF002223","properties":[{"key":"EntryName","value":"PRK01117.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00184","properties":[{"key":"EntryName","value":"purA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11846","properties":[{"key":"EntryName","value":"ADENYLOSUCCINATE SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11846:SF0","properties":[{"key":"EntryName","value":"ADENYLOSUCCINATE SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00709","properties":[{"key":"EntryName","value":"Adenylsucc_synt"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00788","properties":[{"key":"EntryName","value":"Adenylsucc_synt"},{"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":"PS01266","properties":[{"key":"EntryName","value":"ADENYLOSUCCIN_SYN_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00513","properties":[{"key":"EntryName","value":"ADENYLOSUCCIN_SYN_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTSIAVVGSQWGDEGKGKITDFLGTTADLSVRANGGNNAGHTIDFDGKEFKMRLIPSGIFAAKLGAVIGNGVVINPKVLLGELDNLEKSGIDTSNLKISNRAHVIMPYHVMQDTYEEEAKGNLKVGTTKNGIGPTYMDKASRIGIRVCDLIDPETFAEKLRFNLKSKNALFTKVYGKPAMDFDEIYNKYVEYGKRIAKYVCDTSLYVNDALDRDEKVLFEGAQGIMLDIDQGTYPFVSSSNSVSGGIASGSGIGANQIKTVLGICKAYTTRVGAGPFPTELHDETGDKIRDIAHEYGTVTGRPRRVGWFDSVALRHAKRVAGINALSLNLLDVFSGFDKIKICVAYDLNGKQIDYYPASLKEVEACQPVYEELPAWEEDITGAKSWEDLPEKAQAFVKRISEITGIPVVTVSVGPDREQTIVLQDPWTL","length":429,"molWeight":46865,"crc64":"ED7BB977B98EE975","md5":"DC45B22CEFA3AE37BA431B92742E8449"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Active site":3,"Binding site":14},"uniParcId":"UPI00090B7A23"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XUM6","uniProtkbId":"A0ABT1XUM6_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970345.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"GMP synthase [glutamine-hydrolyzing]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"6.3.5.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"GMP synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Glutamine amidotransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"guaA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970345.1"}],"value":"DS743_00315"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002332"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Catalyzes the synthesis of GMP from XMP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"XMP + L-glutamine + ATP + H2O = GMP + L-glutamate + AMP + diphosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11680"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:58115"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.3.5.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005153"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970345.1"}],"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":203,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"GMPS ATP-PPase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51553"}]},{"type":"Active site","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00886"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0332","category":"Biological process","name":"GMP biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970345.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970345.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000011","properties":[{"key":"ProteinId","value":"MCR5970345.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_141372546.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000011.1"}]},{"database":"Proteomes","id":"UP001524940","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:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003921","properties":[{"key":"GoTerm","value":"F:GMP synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01742","properties":[{"key":"EntryName","value":"GATase1_GMP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01997","properties":[{"key":"EntryName","value":"GMP_synthase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.300.10:FF:000002","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000001","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000001","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.300.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00344","properties":[{"key":"EntryName","value":"GMP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR001674","properties":[{"key":"EntryName","value":"GMP_synth_C"}]},{"database":"InterPro","id":"IPR004739","properties":[{"key":"EntryName","value":"GMP_synth_GATase"}]},{"database":"InterPro","id":"IPR022955","properties":[{"key":"EntryName","value":"GMP_synthase"}]},{"database":"InterPro","id":"IPR025777","properties":[{"key":"EntryName","value":"GMPS_ATP_PPase_dom"}]},{"database":"InterPro","id":"IPR022310","properties":[{"key":"EntryName","value":"NAD/GMP_synthase"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"NF000848","properties":[{"key":"EntryName","value":"guaA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00884","properties":[{"key":"EntryName","value":"guaA_Cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00888","properties":[{"key":"EntryName","value":"guaA_Nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11922:SF2","properties":[{"key":"EntryName","value":"GMP SYNTHASE [GLUTAMINE-HYDROLYZING]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11922","properties":[{"key":"EntryName","value":"GMP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00958","properties":[{"key":"EntryName","value":"GMP_synt_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02540","properties":[{"key":"EntryName","value":"NAD_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"PRINTS","id":"PR00096","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51553","properties":[{"key":"EntryName","value":"GMPS_ATP_PPASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAKIDLSNFDKIIVLDFGSQYNQLITRRIRDFGIYSELLPHTITAEEVKKIAPKGIIFSGGPNSVYDENALDVDPEIFELGIPILGICYGMQLMTQKLGGTVEKAGEAEYGSAHIEVKEADSPLYKGLPEKQVVWMSHGDLVTKVPEGFEVLASSKNCPIASMADPDRKFYAIQFHAEVRNSEYGLDILRRFAFDVCGAKDNWTMDDFIKLSVDSIREEVGDANVILGISGGVDSSVTATLLHKAIGSQLTAIFVDHGLLRKNESDEVMAALKEGLGVNIVRVDAKDRFMSKLAGVTDPEKKRKIIGNEFVQVFNDEAKKIKDAKFLVQGTLYTDVIESGTDTAHTIKSHHNVGGLPEDMQFKLIEPLRQLFKDEVRVLGEKLGLPHDLVWRQPFPGPGLAIRVIGEITEEKLRIVRDADAILREEVKNAGLQESIWQYFVALPGMRSVGVMGDGRTYDYAVCIRAVTSIDGMTADFAQIPWDVLQKISVRIVNEVKQVNRVLYDVTSKPPATIEYE","length":517,"molWeight":57405,"crc64":"0CD54A18977163ED","md5":"5A1ABC31C66DD733057D046BB3826B1F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":3,"Binding site":1},"uniParcId":"UPI0011418EA3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XUR4","uniProtkbId":"A0ABT1XUR4_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970397.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Aspartate carbamoyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"2.1.3.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Aspartate transcarbamylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"ATCase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"pyrB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970397.1"}],"value":"DS743_00615"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway"}],"commentType":"FUNCTION"},{"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"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004852"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008896"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970397.1"}],"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":26,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Aspartate/ornithine carbamoyltransferase carbamoyl-P binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02729"}]},{"type":"Domain","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"Aspartate/ornithine carbamoyltransferase Asp/Orn-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00185"}]},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"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_00001"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970397.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970397.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000014","properties":[{"key":"ProteinId","value":"MCR5970397.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_035184388.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000014.1"}]},{"database":"SMR","id":"A0ABT1XUR4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001524940","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-UniRule"}]},{"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-UniRule"}]},{"database":"GO","id":"GO:0006520","properties":[{"key":"GoTerm","value":"P:amino acid metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000011","properties":[{"key":"EntryName","value":"Aspartate carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1370","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00001","properties":[{"key":"EntryName","value":"Asp_carb_tr"},{"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":"NCBIfam","id":"TIGR00670","properties":[{"key":"EntryName","value":"asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002032","properties":[{"key":"EntryName","value":"PRK00856.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753:SF6","properties":[{"key":"EntryName","value":"ASPARTATE CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753","properties":[{"key":"EntryName","value":"ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL"},{"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":"SUPFAM","id":"SSF53671","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00097","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTTVSQNQVVVETEDKQDNLLRLPYFVSVEQLSADDVLHLLQRAQYFKNGGEVPALSRPIFCTNMFFENSTRTHTSFEVAERRLGLTVIPFDPSHSSVNKGENLYDTELTMASLGIELSVIRHPENAYYNEIIRPKEGQHLQMGLVNAGDGSGQHPSQSMLDMMTIYNEFGHFDGLKIMIVGDLTNSRVARSNMEILNTLGAEVYFSGPEYWYNAEEFSKYGTYVKNIDDEIPELDVLMLLRVQHERHNGAEAKTEQLFDAKDYNAAYGLNQRRYDMLKDDAIIMHPGPINRGVEWDGDLVEAPKSRYAVQMHNGVFVRMAMIEAVLRGRKLGGLE","length":336,"molWeight":38135,"crc64":"24CFC94AE1F94FB9","md5":"230738EFB96C94FBB6BB36B123C10CB7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Binding site":10},"uniParcId":"UPI0000358926"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XUS8","uniProtkbId":"A0ABT1XUS8_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970398.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"value":"Dihydroorotase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"value":"DHOase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"value":"3.5.2.3"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"value":"pyrC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970398.1"}],"value":"DS743_00620"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002368"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"value":"Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24296"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30864"},{"database":"ChEBI","id":"CHEBI:32814"}],"ecNumber":"3.5.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010286"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"value":"Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970398.1"}],"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":50,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"Amidohydrolase-related","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01979"}]},{"type":"Active site","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}]},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00220"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970398.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970398.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000014","properties":[{"key":"ProteinId","value":"MCR5970398.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_035184401.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000014.1"}]},{"database":"SMR","id":"A0ABT1XUS8","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001524940","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:0004038","properties":[{"key":"GoTerm","value":"F:allantoinase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004151","properties":[{"key":"GoTerm","value":"F:dihydroorotase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006145","properties":[{"key":"GoTerm","value":"P:purine nucleobase catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01317","properties":[{"key":"EntryName","value":"DHOase_IIa"},{"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":"2.30.40.10","properties":[{"key":"EntryName","value":"Urease, subunit C, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00220_B","properties":[{"key":"EntryName","value":"PyrC_classI_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006680","properties":[{"key":"EntryName","value":"Amidohydro-rel"}]},{"database":"InterPro","id":"IPR004722","properties":[{"key":"EntryName","value":"DHOase"}]},{"database":"InterPro","id":"IPR050138","properties":[{"key":"EntryName","value":"DHOase/Allantoinase_Hydrolase"}]},{"database":"InterPro","id":"IPR002195","properties":[{"key":"EntryName","value":"Dihydroorotase_CS"}]},{"database":"InterPro","id":"IPR011059","properties":[{"key":"EntryName","value":"Metal-dep_hydrolase_composite"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"database":"NCBIfam","id":"NF006837","properties":[{"key":"EntryName","value":"PRK09357.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00857","properties":[{"key":"EntryName","value":"pyrC_multi"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43668","properties":[{"key":"EntryName","value":"ALLANTOINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43668:SF2","properties":[{"key":"EntryName","value":"ALLANTOINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01979","properties":[{"key":"EntryName","value":"Amidohydro_1"},{"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":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00483","properties":[{"key":"EntryName","value":"DIHYDROOROTASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAILLKNGLVYQEGEFIKEDVLISGSKIQAIGLDLPEEGAEVYDLKGKLLAPGLVDIHEHYREPGFTYKETIKTGSEAASRGGFTTVCTMPNVDPIPDDLETFEKQVALNEANSCVHLKQYGAITEDLTSDKVVDMAALKEAGAFAFSNDGHGIQQAGTMYEAMQEAAKVGLAICEHIQDDSLYHHGVMNAGKKAEELGLPGILGVSESAQLARDLVLAQATGVHYHACHVSTKESVELIRIAKEYGINVTAEATPHHLLLSEEEIDGNNGYYKMNPPLRSKEDQFALIEGMLDGTIDLIATDHAPHSREEKAGDMRKAAFGIIGNETAFACLYTKFVKSGQMDLSLLLDLMSYQPAKLFGLDAGVLAPGKEADLAVFDLDHAEKLSEEDYLSKGVNTPFTGQEVYGMTALTFVSGKLVYKSKHFAD","length":427,"molWeight":46319,"crc64":"1AB5BC6163C57E30","md5":"61197606E42173C59FD234E62861C095"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":12},"uniParcId":"UPI0000132C67"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XUU4","uniProtkbId":"A0ABT1XUU4_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970427.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"}],"value":"tRNA (guanine-N(7)-)-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"}],"value":"2.1.1.33"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"}],"value":"tRNA (guanine(46)-N(7))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"}],"value":"tRNA(m7G46)-methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"}],"value":"trmB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970427.1"}],"value":"DS743_00795"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003015"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"}],"value":"Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42708"},{"database":"Rhea","id":"RHEA-COMP:10188"},{"database":"Rhea","id":"RHEA-COMP:10189"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74269"},{"database":"ChEBI","id":"CHEBI:74480"}],"ecNumber":"2.1.1.33","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000142"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00957"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"}],"value":"tRNA modification; N(7)-methylguanine-tRNA biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060767"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00957"}],"value":"Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970427.1"}],"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":"Region","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"Interaction with RNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"}]},{"type":"Active site","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00957"}]},{"type":"Binding site","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00957"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00957"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00957"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00957"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00957"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00957"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"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_01057"}],"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_01057"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01057"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970427.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970427.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000015","properties":[{"key":"ProteinId","value":"MCR5970427.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_002879806.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000015.1"}]},{"database":"GeneID","id":"69669328","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001524940","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0043527","properties":[{"key":"GoTerm","value":"C:tRNA methyltransferase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008176","properties":[{"key":"GoTerm","value":"F:tRNA (guanine(46)-N7)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046500","properties":[{"key":"GoTerm","value":"P:S-adenosylmethionine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02440","properties":[{"key":"EntryName","value":"AdoMet_MTases"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.150:FF:000035","properties":[{"key":"EntryName","value":"tRNA (guanine-N(7)-)-methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.150","properties":[{"key":"EntryName","value":"Vaccinia Virus protein VP39"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01057","properties":[{"key":"EntryName","value":"tRNA_methyltr_TrmB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029063","properties":[{"key":"EntryName","value":"SAM-dependent_MTases_sf"}]},{"database":"InterPro","id":"IPR003358","properties":[{"key":"EntryName","value":"tRNA_(Gua-N-7)_MeTrfase_Trmb"}]},{"database":"InterPro","id":"IPR055361","properties":[{"key":"EntryName","value":"tRNA_methyltr_TrmB_bact"}]},{"database":"NCBIfam","id":"NF001080","properties":[{"key":"EntryName","value":"trmB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00091","properties":[{"key":"EntryName","value":"tRNA (guanosine(46)-N7)-methyltransferase TrmB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23417","properties":[{"key":"EntryName","value":"3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23417:SF14","properties":[{"key":"EntryName","value":"PENTACOTRIPEPTIDE-REPEAT REGION OF PRORP DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02390","properties":[{"key":"EntryName","value":"Methyltransf_4"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53335","properties":[{"key":"EntryName","value":"S-adenosyl-L-methionine-dependent methyltransferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51625","properties":[{"key":"EntryName","value":"SAM_MT_TRMB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRLKNKPWANKLVEEHPESALDWPDPAEKIDWAARFGNDKPIEIEVGSGKGQFITTLAKQHPDRNFVAMEIQKTAAGIILKKKLDEGLDNLQILCADAANLVAYFGENSTSKIYLNFSDPWPKSRHEKRRLTYKDFLAKYQAVLTGDGLIEFKTDNSGLFAYSVKSMNNYGMHFDFVSVDLHHESEEIVEKNVETEYEHKFASKGQPIYCLHAGFLAK","length":218,"molWeight":24812,"crc64":"8752C3DD565B9B20","md5":"5E0E8B69AFC944CC796E2239C71764B9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Active site":1,"Binding site":7},"uniParcId":"UPI0001EC3361"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XUV0","uniProtkbId":"A0ABT1XUV0_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970420.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011971"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Orotate phosphoribosyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"OPRT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"OPRTase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011971"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"2.4.2.10"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"pyrE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970420.1"}],"value":"DS743_00760"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10380"},{"database":"ChEBI","id":"CHEBI:30839"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57538"},{"database":"ChEBI","id":"CHEBI:58017"}],"ecNumber":"2.4.2.10","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004889"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970420.1"}],"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":47,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"Phosphoribosyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00156"}]},{"type":"Binding site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30839"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"orotate","id":"ChEBI:CHEBI:30839"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"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_01208"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970420.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970420.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000015","properties":[{"key":"ProteinId","value":"MCR5970420.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_035184759.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000015.1"}]},{"database":"Proteomes","id":"UP001524940","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004588","properties":[{"key":"GoTerm","value":"F:orotate phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01208","properties":[{"key":"EntryName","value":"PyrE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023031","properties":[{"key":"EntryName","value":"OPRT"}]},{"database":"InterPro","id":"IPR004467","properties":[{"key":"EntryName","value":"Or_phspho_trans_dom"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"NCBIfam","id":"TIGR00336","properties":[{"key":"EntryName","value":"pyrE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19278","properties":[{"key":"EntryName","value":"OROTATE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19278:SF9","properties":[{"key":"EntryName","value":"URIDINE 5'-MONOPHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00156","properties":[{"key":"EntryName","value":"Pribosyltran"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQNNEIIRQLIDKKIVTISTDKDFVYASGMHSPIYTDLRQTISFPKLRQAIAENLAALIKQEFPEVTVIGGVATAGIPHAAWVAQVMNLPMVYIRSKPKDHGQGRQIEGRLSMDDHIVLIDDLISTGGSVLSAVQAVKDTGAHVDGVSSIFTYLLPDADENFKKADTKFAPLLNYRELIEQEIAETVSEEQYKELLAWHQDPWNWKR","length":207,"molWeight":23260,"crc64":"CDDDC2596A0C6A2F","md5":"A4D954F02123D6DB3A8B18AD7D1C8B13"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":5},"uniParcId":"UPI0004AC3502"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XUV8","uniProtkbId":"A0ABT1XUV8_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970421.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"value":"Orotidine 5'-phosphate decarboxylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"value":"4.1.1.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"value":"OMP decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"value":"OMPDCase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"value":"OMPdecase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"value":"pyrF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970421.1"}],"value":"DS743_00765"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002356"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"value":"Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"orotidine 5'-phosphate + H(+) = UMP + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11596"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57538"},{"database":"ChEBI","id":"CHEBI:57865"}],"ecNumber":"4.1.1.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10110"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000512"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004861"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000512"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061012"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"value":"Belongs to the OMP decarboxylase family. Type 1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970421.1"}],"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":230,"modifier":"EXACT"}},"description":"Orotidine 5'-phosphate decarboxylase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00934"}]},{"type":"Active site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"For OMPdecase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR614732-1"}]},{"type":"Active site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"For OMPdecase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR614732-1"}]},{"type":"Active site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10110"}]},{"type":"Active site","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"For OMPdecase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR614732-1"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR614732-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR614732-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR614732-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR614732-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR614732-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR614732-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR614732-2"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01200"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970421.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970421.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000015","properties":[{"key":"ProteinId","value":"MCR5970421.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_013439932.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000015.1"}]},{"database":"Proteomes","id":"UP001524940","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:0004590","properties":[{"key":"GoTerm","value":"F:orotidine-5'-phosphate decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"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-UniRule"}]},{"database":"CDD","id":"cd04725","properties":[{"key":"EntryName","value":"OMP_decarboxylase_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000015","properties":[{"key":"EntryName","value":"Orotidine 5'-phosphate decarboxylase"},{"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_01200_B","properties":[{"key":"EntryName","value":"OMPdecase_type1_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR014732","properties":[{"key":"EntryName","value":"OMPdecase"}]},{"database":"InterPro","id":"IPR018089","properties":[{"key":"EntryName","value":"OMPdecase_AS"}]},{"database":"InterPro","id":"IPR047596","properties":[{"key":"EntryName","value":"OMPdecase_bac"}]},{"database":"InterPro","id":"IPR001754","properties":[{"key":"EntryName","value":"OMPdeCOase_dom"}]},{"database":"InterPro","id":"IPR011060","properties":[{"key":"EntryName","value":"RibuloseP-bd_barrel"}]},{"database":"NCBIfam","id":"NF001273","properties":[{"key":"EntryName","value":"pyrF"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01740","properties":[{"key":"EntryName","value":"pyrF"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32119","properties":[{"key":"EntryName","value":"OROTIDINE 5'-PHOSPHATE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32119:SF2","properties":[{"key":"EntryName","value":"OROTIDINE 5'-PHOSPHATE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00215","properties":[{"key":"EntryName","value":"OMPdecase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00934","properties":[{"key":"EntryName","value":"OMPdecase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51366","properties":[{"key":"EntryName","value":"Ribulose-phoshate binding barrel"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00156","properties":[{"key":"EntryName","value":"OMPDECASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNKPLFIALDYDDQEKMWLFLNQLKDKQGLHVKLGMEMFYQYGPEIVRDLSAKGYQIFLDLKLHDIPNTVKRTAHQLAALGVYCTTVHALGGKQMIQAAKEGLIEGTPAGKPVPKLLAVTELTSISEEVLKNEQHCSLNLADEVKSLAHQAQEAGADGIICSPLEVKAMKSEFNDDFMFVTPGIRPKSYQKDDQARVATPGQARENGSTAIVVGRPITQAADPQKAYEEILKDWSKNDAK","length":240,"molWeight":26582,"crc64":"71DA4ACFE52AF888","md5":"E997E9713D3DF9E32C0593BB6945790D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":4,"Binding site":8},"uniParcId":"UPI0001EC3368"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XUW8","uniProtkbId":"A0ABT1XUW8_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970439.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Lipoprotein signal peptidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"3.4.23.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Prolipoprotein signal peptidase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Signal peptidase II"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"SPase II"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"lspA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970439.1"}],"value":"DS743_00855"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"This protein specifically catalyzes the removal of signal peptides from prolipoproteins"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.","ecNumber":"3.4.23.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Protein modification; lipoprotein biosynthesis (signal peptide cleavage)"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006139"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004181"}],"value":"Belongs to the peptidase A8 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970439.1"}],"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":60,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]},{"type":"Transmembrane","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]},{"type":"Transmembrane","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]},{"type":"Active site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]},{"type":"Active site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022750"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-0064","category":"Molecular function","name":"Aspartyl protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00161"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970439.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970439.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000016","properties":[{"key":"ProteinId","value":"MCR5970439.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_002876847.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000016.1"}]},{"database":"GeneID","id":"69668944","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001524940","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004190","properties":[{"key":"GoTerm","value":"F:aspartic-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"HAMAP","id":"MF_00161","properties":[{"key":"EntryName","value":"LspA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001872","properties":[{"key":"EntryName","value":"Peptidase_A8"}]},{"database":"NCBIfam","id":"TIGR00077","properties":[{"key":"EntryName","value":"lspA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33695","properties":[{"key":"EntryName","value":"LIPOPROTEIN SIGNAL PEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33695:SF1","properties":[{"key":"EntryName","value":"LIPOPROTEIN SIGNAL PEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01252","properties":[{"key":"EntryName","value":"Peptidase_A8"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00781","properties":[{"key":"EntryName","value":"LIPOSIGPTASE"}]}],"sequence":{"value":"MQIVGLVIAALIAAADQALKYYIVTNYRLGEVHDVMPGLFSFTYIQNNGAAWNILSGKMWFFYVVSSVAIAVVLYYYFNKKYSHWMFKSGLVLVLGGIIGNLIDRLHLKYVIDMIQLDFVQFNIFNLADAAITVGVILIFSYLLFIERED","length":150,"molWeight":17093,"crc64":"134751870B21FEF7","md5":"7916AE09DD09A8167099DE2DA3406860"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Transmembrane":3,"Active site":2},"uniParcId":"UPI0001EC3120"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABT1XUX7","uniProtkbId":"A0ABT1XUX7_LACLE","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Lactobacillus leichmannii","taxonId":28039,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970456.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Lactobacillaceae","Lactobacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Serine--tRNA ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"6.1.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Seryl-tRNA synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"SerRS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Seryl-tRNA(Ser/Sec) synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"serS"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970456.1"}],"value":"DS743_00945"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tRNA(Sec) + L-serine + ATP = L-seryl-tRNA(Sec) + AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42580"},{"database":"Rhea","id":"RHEA-COMP:9742"},{"database":"Rhea","id":"RHEA-COMP:10128"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78533"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.1.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047929"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12292"},{"database":"Rhea","id":"RHEA-COMP:9669"},{"database":"Rhea","id":"RHEA-COMP:9703"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78533"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.1.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048823"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005045"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Homodimer. The tRNA molecule binds across the dimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970456.1"}],"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":173,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"Aminoacyl-transfer RNA synthetases class-II family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50862"}]},{"type":"Coiled coil","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Binding site","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}},{"type":"Binding site","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-1"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-1"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-1"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}},{"type":"Binding site","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-1"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}},{"type":"Binding site","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023146"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0030","category":"Molecular function","name":"Aminoacyl-tRNA synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-KQ9094QJBBLT","citationType":"submission","authors":["Rong J.-C.","Li M.-Y.","Zhang Q.-F.","Chi N.-Y."],"title":"Genome sequencing and assembly of Lactobacillus leichmannii.","publicationDate":"JUL-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970456.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}],"value":"JCM 1148","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MCR5970456.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001524940"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"QOCY01000017","properties":[{"key":"ProteinId","value":"MCR5970456.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_035185202.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_QOCY01000017.1"}]},{"database":"Proteomes","id":"UP001524940","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:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0140096","properties":[{"key":"GoTerm","value":"F:catalytic activity, acting on a protein"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0004828","properties":[{"key":"GoTerm","value":"F:serine-tRNA ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016260","properties":[{"key":"GoTerm","value":"P:L-selenocysteine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006434","properties":[{"key":"GoTerm","value":"P:seryl-tRNA aminoacylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00770","properties":[{"key":"EntryName","value":"SerRS_core"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.930.10","properties":[{"key":"EntryName","value":"Bira Bifunctional Protein, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.287.40","properties":[{"key":"EntryName","value":"Serine-tRNA synthetase, tRNA binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00176","properties":[{"key":"EntryName","value":"Ser_tRNA_synth_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002314","properties":[{"key":"EntryName","value":"aa-tRNA-synt_IIb"}]},{"database":"InterPro","id":"IPR006195","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II"}]},{"database":"InterPro","id":"IPR045864","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II/BPL/LPL"}]},{"database":"InterPro","id":"IPR002317","properties":[{"key":"EntryName","value":"Ser-tRNA-ligase_type_1"}]},{"database":"InterPro","id":"IPR015866","properties":[{"key":"EntryName","value":"Ser-tRNA-synth_1_N"}]},{"database":"InterPro","id":"IPR042103","properties":[{"key":"EntryName","value":"SerRS_1_N_sf"}]},{"database":"InterPro","id":"IPR033729","properties":[{"key":"EntryName","value":"SerRS_core"}]},{"database":"InterPro","id":"IPR010978","properties":[{"key":"EntryName","value":"tRNA-bd_arm"}]},{"database":"NCBIfam","id":"TIGR00414","properties":[{"key":"EntryName","value":"serS"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43697:SF1","properties":[{"key":"EntryName","value":"SERINE--TRNA LIGASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43697","properties":[{"key":"EntryName","value":"SERYL-TRNA SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02403","properties":[{"key":"EntryName","value":"Seryl_tRNA_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00587","properties":[{"key":"EntryName","value":"tRNA-synt_2b"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001529","properties":[{"key":"EntryName","value":"Ser-tRNA-synth_IIa"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00981","properties":[{"key":"EntryName","value":"TRNASYNTHSER"}]},{"database":"SUPFAM","id":"SSF55681","properties":[{"key":"EntryName","value":"Class II aaRS and biotin synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46589","properties":[{"key":"EntryName","value":"tRNA-binding arm"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50862","properties":[{"key":"EntryName","value":"AA_TRNA_LIGASE_II"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLDIKVIRENLDWAKEKLATRGIKPEQLDELVAIDAKRREAMVQCENLKAERNEVSKKIAAAKREKADASEAIANMREVGAKIKELDKEVDELQEKQEYILLRLPNFPADSDPIGPDESYNEEVRRWNELTKFDYQPKAHWDLGTDLNILDWDAASKVSAARFVYYKGAGALLERAVYNFFLDENTSEGYTEVITPSLVNNDSMQGTGQFPKFTEDVYTIVDNDDPEVARNLTLIPTAEVPLVNYFRGDIIDGKNLPINVTALSPAFRSEAGSAGRDTRGLIRMHEFRKVEMVKVVKPEDSWKELENLTHNAEHLLQKLGLPYRVVALSTGDASFTSAKTYDLEVWMPAQDTYREISSCSNCTDFQARRAQIRYRDEDGKVKLTHTLNGSGLAVGRTVAAILENYQNEDGTVTVPEALRPYMHGMTKITPEVKWH","length":435,"molWeight":49250,"crc64":"4D2136960316AAEB","md5":"DFDCD2A77291DBCFFFD354BE23A2521B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Coiled coil":1,"Binding site":8},"uniParcId":"UPI0004AC3887"}}]}