{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6RCU0","uniProtkbId":"I6RCU0_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-10-03","entryVersion":49,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44653.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"value":"Transaldolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"value":"2.2.1.2"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"value":"tal"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"value":"Transaldolase involved in the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedoheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate. Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17053"},{"database":"ChEBI","id":"CHEBI:16897"},{"database":"ChEBI","id":"CHEBI:57483"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:59776"}],"ecNumber":"2.2.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10019"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"value":"Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005740"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"value":"Belongs to the transaldolase family. Type 3B subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}]},{"type":"Active site","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10019"}]},{"type":"Active site","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"Nucleophile; Schiff-base intermediate with substrate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}]},{"type":"Binding site","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":6,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023126"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"id":"KW-0570","category":"Biological process","name":"Pentose shunt"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023270"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"id":"KW-0704","category":"Ligand","name":"Schiff base"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00494"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44653.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44653.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44653.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6RCU0","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00115","properties":[{"key":"RectionId","value":"UER00414"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0016832","properties":[{"key":"GoTerm","value":"F:aldehyde-lyase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004801","properties":[{"key":"GoTerm","value":"F:transaldolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006098","properties":[{"key":"GoTerm","value":"P:pentose-phosphate shunt"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00956","properties":[{"key":"EntryName","value":"Transaldolase_FSA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000018","properties":[{"key":"EntryName","value":"Probable transaldolase"},{"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_00494","properties":[{"key":"EntryName","value":"Transaldolase_3b"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR001585","properties":[{"key":"EntryName","value":"TAL/FSA"}]},{"database":"InterPro","id":"IPR022999","properties":[{"key":"EntryName","value":"Transaldolase_3B"}]},{"database":"InterPro","id":"IPR004731","properties":[{"key":"EntryName","value":"Transaldolase_3B/F6P_aldolase"}]},{"database":"InterPro","id":"IPR018225","properties":[{"key":"EntryName","value":"Transaldolase_AS"}]},{"database":"InterPro","id":"IPR033919","properties":[{"key":"EntryName","value":"TSA/FSA_arc/bac"}]},{"database":"NCBIfam","id":"TIGR00875","properties":[{"key":"EntryName","value":"fsa_talC_mipB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10683","properties":[{"key":"EntryName","value":"TRANSALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10683:SF36","properties":[{"key":"EntryName","value":"TRANSALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00923","properties":[{"key":"EntryName","value":"TAL_FSA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01054","properties":[{"key":"EntryName","value":"TRANSALDOLASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00958","properties":[{"key":"EntryName","value":"TRANSALDOLASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKFFIDTANVEEIKEANDLGVISGVTTNPSLVAKEGRDFIEVIKEIASIIDGPISAEVISEDHQGMIQEARKLAAIHNNIVIKIPMTAEGLKAVKALSKEGIKTNVTLIFSANQALLAARAGATYVSPFVGRLDDISTEGMQLIRDIVEIFKNYDISTEIIVASVRHPMHVLKAAKLGAHIATVPYKVIMQMIKHPLTDAGIQRFKEDWKKANLKI","length":216,"molWeight":23684,"crc64":"1002B128E429B657","md5":"D48BEECC57CFC4723B4D0695897CEE9C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Active site":3,"Binding site":8},"uniParcId":"UPI0002680B51"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6QQS2","uniProtkbId":"I6QQS2_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2012-10-03","entryVersion":49,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44652.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364073"}],"value":"Xylulose kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364073"}],"value":"Xylulokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364073"}],"value":"2.7.1.17"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44652.1"}],"value":"xylK"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364073"}],"value":"xylB"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"}],"value":"Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-xylulose + ATP = D-xylulose 5-phosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10964"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17140"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57737"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364073"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009156"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003733"}],"value":"Belongs to the FGGY kinase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"Carbohydrate kinase FGGY N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00370"}]},{"type":"Domain","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"Carbohydrate kinase FGGY C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02782"}]},{"type":"Active site","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"}]},{"type":"Binding site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":8,"modifier":"EXACT"}},"description":"Important for activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022629"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02220"}],"id":"KW-0859","category":"Biological process","name":"Xylose metabolism"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44652.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44652.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44652.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6QQS2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004856","properties":[{"key":"GoTerm","value":"F:D-xylulokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005998","properties":[{"key":"GoTerm","value":"P:xylulose catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd07808","properties":[{"key":"EntryName","value":"ASKHA_NBD_FGGY_EcXK-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_02220","properties":[{"key":"EntryName","value":"XylB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"InterPro","id":"IPR000577","properties":[{"key":"EntryName","value":"Carb_kinase_FGGY"}]},{"database":"InterPro","id":"IPR018483","properties":[{"key":"EntryName","value":"Carb_kinase_FGGY_CS"}]},{"database":"InterPro","id":"IPR018485","properties":[{"key":"EntryName","value":"FGGY_C"}]},{"database":"InterPro","id":"IPR050406","properties":[{"key":"EntryName","value":"FGGY_Carb_Kinase"}]},{"database":"InterPro","id":"IPR018484","properties":[{"key":"EntryName","value":"FGGY_N"}]},{"database":"InterPro","id":"IPR006000","properties":[{"key":"EntryName","value":"Xylulokinase"}]},{"database":"NCBIfam","id":"TIGR01312","properties":[{"key":"EntryName","value":"XylB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43095","properties":[{"key":"EntryName","value":"SUGAR KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43095:SF5","properties":[{"key":"EntryName","value":"XYLULOSE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02782","properties":[{"key":"EntryName","value":"FGGY_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00370","properties":[{"key":"EntryName","value":"FGGY_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000538","properties":[{"key":"EntryName","value":"GlpK"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00933","properties":[{"key":"EntryName","value":"FGGY_KINASES_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00445","properties":[{"key":"EntryName","value":"FGGY_KINASES_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSYLIGIDIGTSGTKTVLFDERGNTVASSTVEYDMAQPEIGWAEQDPEDWWKATCQSLREVIGKSGINVDEIKGIGLSGQMHGAVLLDKDGNVLRSAIIWCDQRSSAECEEITDIIGYGRLIELAANPALTGFTAPKVMWVKKHQPEIFEKIAHILLPKDYIRYRLTGEFATEVSDASGTLFLNVKERKWSREIVEKLGLNIEWLPEVYESHVVSGKVCKKAAESTGLKEGTPVVGGGGDQAAGAVGNGIVKKGLVSSTIGTSGVVFAYTDKVTIDPKGRVHTFCHAIPDTWHVMGVTQGAGLSLKWWRDNFGFEEKTLGSLTGTDPYVYMDKEAEQAQPGCGGLIYLPYLMGERTPHLDPYAKGVFFGLTAKHRRQEVIRSVLEGVVFSLRDCLEIIKGMGIPVEEIRASGGGGRSRIWRQIQADVFKTDIVTINSAEGPALGVALLAGVGTGLYSSVVEACDAVIKRVSVQHPNQSLFDVYEKNYRLYTALYPAVKDLYRL","length":503,"molWeight":54999,"crc64":"AED04C43E86E597B","md5":"45DA9A7742195E7C022691FF3CFD6637"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":1,"Site":1},"uniParcId":"UPI0002680B50"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6QTZ4","uniProtkbId":"I6QTZ4_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2012-10-03","entryVersion":36,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44650.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361198"}],"value":"Xylan alpha-1,2-glucuronidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361198"}],"value":"3.2.1.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44650.1"}],"value":"agu67A"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-O-methyl-alpha-D-glucuronosyl-(1->2)-beta-D-xylosyl-(1->4)-beta-D-xylosyl-(1->4)-beta-D-xylose + H2O = beta-D-xylotriose + 4-O-methyl-beta-D-glucuronate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:84887"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:62797"},{"database":"ChEBI","id":"CHEBI:234000"},{"database":"ChEBI","id":"CHEBI:234015"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361198"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:84888"},"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361198"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361198"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008833"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR029900"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361198"}],"value":"Belongs to the glycosyl hydrolase 67 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Alpha glucuronidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03648"}]},{"type":"Domain","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":464,"modifier":"EXACT"}},"description":"Glycosyl hydrolase family 67 catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF07488"}]},{"type":"Domain","location":{"start":{"value":465,"modifier":"EXACT"},"end":{"value":687,"modifier":"EXACT"}},"description":"Glycosyl hydrolase family 67 C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF07477"}]},{"type":"Active site","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR029900-1"}]},{"type":"Active site","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR029900-1"}]},{"type":"Active site","location":{"start":{"value":404,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR029900-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361198"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023295"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR029900"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR029900"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023326"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361198"}],"id":"KW-0624","category":"Biological process","name":"Polysaccharide degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022651"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR029900"}],"id":"KW-0858","category":"Biological process","name":"Xylan degradation"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44650.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44650.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44650.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6QTZ4","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH67","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 67"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046559","properties":[{"key":"GoTerm","value":"F:alpha-glucuronidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033939","properties":[{"key":"GoTerm","value":"F:xylan alpha-1,2-glucuronosidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:2000886","properties":[{"key":"GoTerm","value":"P:glucuronoxylan catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"FunFam","id":"3.20.20.80:FF:000096","properties":[{"key":"EntryName","value":"Xylan alpha-1,2-glucuronidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1330.10","properties":[{"key":"EntryName","value":"Alpha-glucuronidase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.379.10","properties":[{"key":"EntryName","value":"Chitobiase/beta-hexosaminidase domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR037054","properties":[{"key":"EntryName","value":"A-glucoronidase_C_sf"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR011395","properties":[{"key":"EntryName","value":"Glyco_hydro_67_aGlcAse"}]},{"database":"InterPro","id":"IPR005154","properties":[{"key":"EntryName","value":"Glyco_hydro_67_aGlcAse_N"}]},{"database":"InterPro","id":"IPR011099","properties":[{"key":"EntryName","value":"Glyco_hydro_67_C"}]},{"database":"InterPro","id":"IPR011100","properties":[{"key":"EntryName","value":"Glyco_hydro_67_cat"}]},{"database":"InterPro","id":"IPR029018","properties":[{"key":"EntryName","value":"Hex-like_dom2"}]},{"database":"PANTHER","id":"PTHR39207","properties":[{"key":"EntryName","value":"ALPHA-GLUCURONIDASE A"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39207:SF1","properties":[{"key":"EntryName","value":"ALPHA-GLUCURONIDASE A"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07477","properties":[{"key":"EntryName","value":"Glyco_hydro_67C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07488","properties":[{"key":"EntryName","value":"Glyco_hydro_67M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03648","properties":[{"key":"EntryName","value":"Glyco_hydro_67N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF029900","properties":[{"key":"EntryName","value":"Alpha-glucuronds"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55545","properties":[{"key":"EntryName","value":"beta-N-acetylhexosaminidase-like domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDKEVDYSLCWLEYSKIDDEPYREKLSKVVKNIIAVGQDKFTQTAVEELKTAVTSLVGFEPEVSKEALCGDNPISGIIVGNVTDALIMKYISDDEIQKLDEEGYVIKSVKENPGLVVIGSKNGHGLVYGAFSFIKHIQLKRDVEEVHIIDNPKCKLRLLNHWDNMDGTVERGYAGRSIFFCDNKVTNSLGRIKDYARLLSSIGINGVVINNVNVNKNAIWLITPKYLGDLAKLADVFRQYGIKIYLSINFASPIYIGKLKTADPLDEDVIKWWKETAKTIYEYIPDFGGFLVKADSEFNPGPYKFGRDHADGANMLAEALAPYGGIVIWRCFVYNCTQDWRDTKTDRAKAAYDIFKPLDGKFAENVVLQVKYGPMDFQVREPVSPLFGGLERTNQLIELQITQEYTGQQIDLCYLATMWKEVLEFDTYAKGPESKVKYVVDGTLFNNKYSGFAGVSNVGSDKNWTGHWLAQANLYAFGMLAWDHSFTPEEIAREWCVRALTNDPFAVETIVSMLMRSWRVYEKYTAPLGIGWMVTPHTHYGPSVDGYEYSKWGTYHRADTKAIGIDRSVKSGTGFAGQYHRENAAMFESMETCPEELLLFFHRVPYDYVLKSGETLIQHIYNTHFEGAEEAEKLKEDWVKIKDYIRKDIYEDVLERFNRQIENAKEWRDVVNSYFYRKTGIPDKYGRKIY","length":690,"molWeight":78976,"crc64":"09D9502DB501ECFE","md5":"AABE14189BEBE6C99CCEC84A9F0E9835"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":3,"Active site":3},"uniParcId":"UPI0002680B4D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6R6Y0","uniProtkbId":"I6R6Y0_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-10-03","entryVersion":57,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44654.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00018672"}],"value":"Stage 0 sporulation protein A homolog"}}},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024867"}],"value":"May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00593"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Response regulatory","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50110"}]},{"type":"Domain","location":{"start":{"value":431,"modifier":"EXACT"},"end":{"value":494,"modifier":"EXACT"}},"description":"HTH araC/xylS-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS01124"}]},{"type":"DNA binding","location":{"start":{"value":449,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"H-T-H motif","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00593"}]},{"type":"Coiled coil","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Modified residue","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"4-aspartylphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00169"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00593"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00169"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00593"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00593"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023012"}],"id":"KW-0902","category":"Biological process","name":"Two-component regulatory system"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44654.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44654.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44654.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6R6Y0","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:0003700","properties":[{"key":"GoTerm","value":"F:DNA-binding transcription factor activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043565","properties":[{"key":"GoTerm","value":"F:sequence-specific DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000160","properties":[{"key":"GoTerm","value":"P:phosphorelay signal transduction system"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd17536","properties":[{"key":"EntryName","value":"REC_YesN-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2300","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.60","properties":[{"key":"EntryName","value":"Homeodomain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR041522","properties":[{"key":"EntryName","value":"CdaR_GGDEF"}]},{"database":"InterPro","id":"IPR011006","properties":[{"key":"EntryName","value":"CheY-like_sf"}]},{"database":"InterPro","id":"IPR009057","properties":[{"key":"EntryName","value":"Homeodomain-like_sf"}]},{"database":"InterPro","id":"IPR051552","properties":[{"key":"EntryName","value":"HptR"}]},{"database":"InterPro","id":"IPR018060","properties":[{"key":"EntryName","value":"HTH_AraC"}]},{"database":"InterPro","id":"IPR001789","properties":[{"key":"EntryName","value":"Sig_transdc_resp-reg_receiver"}]},{"database":"PANTHER","id":"PTHR42713","properties":[{"key":"EntryName","value":"HISTIDINE KINASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42713:SF3","properties":[{"key":"EntryName","value":"TRANSCRIPTIONAL REGULATORY PROTEIN HPTR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17853","properties":[{"key":"EntryName","value":"GGDEF_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00072","properties":[{"key":"EntryName","value":"Response_reg"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00448","properties":[{"key":"EntryName","value":"REC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52172","properties":[{"key":"EntryName","value":"CheY-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46689","properties":[{"key":"EntryName","value":"Homeodomain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01124","properties":[{"key":"EntryName","value":"HTH_ARAC_FAMILY_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50110","properties":[{"key":"EntryName","value":"RESPONSE_REGULATORY"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIKDKIKVLIIDDEYLERNLLKGCIDWDMLGMEIVGEASNAEEGFKLIDEFKPNVVFTDIKMPGIDGIKFSESILQKYPTIKIVVVTGYNDFVYAQKSVKIGVSDFLLKPIDEDEVLNTVYKLKAVIENERKKKEEFEELKRQLYDNLPYLKERFLNELINGNLDDNLVKEKLEFFDIPLNGSIYQVAVLEIINSNDVNEESRLIQNFKVINYVKSYFKELRRIMVFADSMNRIIILNNDEKLDLYKTCIRLKNKIIRDVDCIVNIGIGNIKGRISDIKVSYEEAIDALNYRIAVGNNSVIHYRDVQFTESKTGLDTNHLFNELRFYLKSGLENNAINVVKDIFSNLDLKSENAIKLIRVTALNVISICFTVSLELKENFDDIYLSEVESYNKIINIETLPDMIEYISTIVRNTIKAINKEQINNINNLIANVKKFIEENIGDSNLSLSYVAKHFYLNPSYLSRTFKKETGINFIEYLTNKRMEKAINLIKEKT","length":494,"molWeight":57265,"crc64":"A757F248FA05A55F","md5":"E642E442C132DCBB8AB07EF0C83E49BE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"DNA binding":1,"Coiled coil":1,"Modified residue":1},"uniParcId":"UPI0002680B53"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"J7JXS8","uniProtkbId":"J7JXS8_9THEO","entryAudit":{"firstPublicDate":"2012-10-31","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-10-31","entryVersion":45,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFQ62797.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361174"}],"value":"Beta-xylanase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361174"}],"value":"3.2.1.8"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFQ62797.1"}],"value":"xyn10A"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.","ecNumber":"3.2.1.8","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01096"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361174"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01096"}],"value":"Glycan degradation; xylan degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007495"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01096"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361174"}],"value":"Belongs to the glycosyl hydrolase 10 (cellulase F) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":1454,"modifier":"EXACT"}},"description":"Beta-xylanase","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5003793785"},{"type":"Domain","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":692,"modifier":"EXACT"}},"description":"GH10","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51760"}]},{"type":"Domain","location":{"start":{"value":1270,"modifier":"EXACT"},"end":{"value":1333,"modifier":"EXACT"}},"description":"SLH","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51272"}]},{"type":"Domain","location":{"start":{"value":1334,"modifier":"EXACT"},"end":{"value":1392,"modifier":"EXACT"}},"description":"SLH","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51272"}]},{"type":"Domain","location":{"start":{"value":1395,"modifier":"EXACT"},"end":{"value":1454,"modifier":"EXACT"}},"description":"SLH","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51272"}]},{"type":"Region","location":{"start":{"value":1065,"modifier":"EXACT"},"end":{"value":1086,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1065,"modifier":"EXACT"},"end":{"value":1076,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":512,"modifier":"EXACT"},"end":{"value":512,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01096"}]},{"type":"Active site","location":{"start":{"value":617,"modifier":"EXACT"},"end":{"value":617,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10061"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01096"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023295"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01096"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01096"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023326"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01096"}],"id":"KW-0624","category":"Biological process","name":"Polysaccharide degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01096"}],"id":"KW-0858","category":"Biological process","name":"Xylan degradation"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFQ62797.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFQ62797.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX271581","properties":[{"key":"ProteinId","value":"AFQ62797.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"SMR","id":"J7JXS8","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"CBM22","properties":[{"key":"FamilyName","value":"Carbohydrate-Binding Module Family 22"}]},{"database":"CAZy","id":"CBM9","properties":[{"key":"FamilyName","value":"Carbohydrate-Binding Module Family 9"}]},{"database":"CAZy","id":"GH10","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 10"}]},{"database":"GO","id":"GO:0030246","properties":[{"key":"GoTerm","value":"F:carbohydrate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0031176","properties":[{"key":"GoTerm","value":"F:endo-1,4-beta-xylanase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0045493","properties":[{"key":"GoTerm","value":"P:xylan catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00005","properties":[{"key":"EntryName","value":"CBM9_like_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.1190","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.60.120.260","properties":[{"key":"EntryName","value":"Galactose-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR010502","properties":[{"key":"EntryName","value":"Carb-bd_dom_fam9"}]},{"database":"InterPro","id":"IPR003305","properties":[{"key":"EntryName","value":"CenC_carb-bd"}]},{"database":"InterPro","id":"IPR008979","properties":[{"key":"EntryName","value":"Galactose-bd-like_sf"}]},{"database":"InterPro","id":"IPR044846","properties":[{"key":"EntryName","value":"GH10"}]},{"database":"InterPro","id":"IPR031158","properties":[{"key":"EntryName","value":"GH10_AS"}]},{"database":"InterPro","id":"IPR001000","properties":[{"key":"EntryName","value":"GH10_dom"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR018087","properties":[{"key":"EntryName","value":"Glyco_hydro_5_CS"}]},{"database":"InterPro","id":"IPR001119","properties":[{"key":"EntryName","value":"SLH_dom"}]},{"database":"PANTHER","id":"PTHR31490:SF90","properties":[{"key":"EntryName","value":"ENDO-1,4-BETA-XYLANASE A"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31490","properties":[{"key":"EntryName","value":"GLYCOSYL HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06452","properties":[{"key":"EntryName","value":"CBM9_1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02018","properties":[{"key":"EntryName","value":"CBM_4_9"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00331","properties":[{"key":"EntryName","value":"Glyco_hydro_10"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00395","properties":[{"key":"EntryName","value":"SLH"},{"key":"MatchStatus","value":"3"}]},{"database":"PRINTS","id":"PR00134","properties":[{"key":"EntryName","value":"GLHYDRLASE10"}]},{"database":"SMART","id":"SM00633","properties":[{"key":"EntryName","value":"Glyco_10"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49344","properties":[{"key":"EntryName","value":"CBD9-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF49785","properties":[{"key":"EntryName","value":"Galactose-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00591","properties":[{"key":"EntryName","value":"GH10_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51760","properties":[{"key":"EntryName","value":"GH10_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00659","properties":[{"key":"EntryName","value":"GLYCOSYL_HYDROL_F5"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51272","properties":[{"key":"EntryName","value":"SLH"},{"key":"MatchStatus","value":"3"}]}],"sequence":{"value":"MSMKKRKMLSLLVSFMLLITAFMPVNKVVAAKLPDASGNLSVNLVVNGDFESGNIDGWTKHGNPTLEITSEQAIGNYSLKVTGRTQTYEGPAYDLLGKMENGKTYNITLKVRAVSGQIAMGHPNPPKITVTMRRKYIPNTEGDTGSYYDTIAWQKPIDESSWTTISGSYTLSYNGTLTELFMYVESPDPTLEYYIDDVTITPLDAPMIKNVVDNSTFENGSAAGWTGTGGCSVSSVSEEHHSGDYSLKTTGRTSSWMGPSYNLLGKIVPGKQYSVDFWVKYNSGINPTEQFKATVKATPTEGSPNYIQVNDPVTVDQGQWVEIKGTFTLPTGNYSGINIYVETPNPTLDFYIDDFTVTGEAASTSTKIQENIPDLHSVFSDYFPIGVAVEPNRLADSDPHSQLVAKHFNMLVAENAMKPISLEPTEGNFTFNNADAIVDFAIAHNMKMRGHTLLWHNQVPDWFFQDPSDPSKPASRDLLLQRLQTYITTVLNHFKTKYSSNNPIVAWDVVNEVLDDNGNLRNSKWLQIIGPDYIEKAFQYAHEADPNVKLFINDYNIENNGAKTQAMYNLVKKLKDEGIPVDGIGMQMHININSNVDNIKASIEKFASLGVQIQITELDMNMQGNVSQDALLRQARLYKQLFDVLKQEKQYITAVVFWGVSDDVTWLSQPNAPLLFDSNLQAKPAYWAIVDPNKAAVNRQAAQASQGSPSIGTGVDKDWITAKSLNVNTFVKGINGATAKVKTLWDSKNLYVLAQVVDNTPAANDSIELFVDKNGDKSTTYQPDDKHYIIYRDNSGSSDITHYVQSDEYGYTVQAAIPLGDVNPQVGAKIGFDVRVNDDKGSGTVDSIAVWNDYSNAQDVSTAYYGDLTLSKPSQITEAVYGTPTIDGKIDSIWDQANVINTNVWVQGTSGATAKVRTMWDNHYLYVLAEVTDSNLNKSSPNPYEQDSVEVFLDQNDHKTSYYENDDGQYRVNYDNEQSFGGSTNSQGFKSATSKTSTGYIVEEAIPFTAITPTDGQILGFDVQVNDADASGRRTSIVTWCDASGNSWQDTSGFGNLMLVDTRQLPRSGSNSNNLGDNERNSSDMGTVTKTADTVTLVLNEIEALNVVKNSSSNVITFDISNIGTTLQKVLEIPVSVLNAAKNLNKEIIVKSGFVSATISRGSLDLSNVSGNIKISIKDNGKYDRTSGFIPVTNALDVLIKAGNEDVKILKPLEITLDVPTSGINDLRKVGVYFYNEATGEWEYIGGKIDKDDNVITFEANNSSIYAAFEYDKTFADVKNHWAKDAIEVLASRHIAKGIDGKNFAPDKAVTRAEFAAMITRLLGIPEREYKGEFIDVKAGDWYANAIEAAYEAGIMLGDGKRMRPNDYITREEIAAISMRAFGKLTSYDEEQFSKTTFADDDRVSDWAKKAVANAKKAGIMEGVSGDLFAPKENATRAEAAVVIYRILDKSGSF","length":1454,"molWeight":160055,"crc64":"2B9D70744C83CBF0","md5":"58CCB490205341A1A21C865AEE13137D"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":4,"Region":1,"Compositional bias":1,"Active site":2},"uniParcId":"UPI00027EF31B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"L0E2M2","uniProtkbId":"L0E2M2_9THEO","entryAudit":{"firstPublicDate":"2013-03-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-03-06","entryVersion":42,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35557.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35557.1"}],"value":"MBP1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35557.1"}],"value":"mbp1"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008520"}],"value":"Belongs to the bacterial solute-binding protein 1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":447,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5050004429"},{"type":"Binding site","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9G"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9G"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9G"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"3"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9G"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"3"}},{"type":"Binding site","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9G"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"4"}},{"type":"Binding site","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9G"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"4"}},{"type":"Binding site","location":{"start":{"value":413,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9G"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"3"}},{"type":"Lipidation","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9F"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9G"}],"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9G"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0564","category":"PTM","name":"Palmitate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"}],"id":"KW-0813","category":"Biological process","name":"Transport"},{"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9G"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"20562312","citationType":"journal article","authors":["Han Y.","Dodd D.","Hespen C.W.","Ohene-Adjei S.","Schroeder C.M.","Mackie R.I.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"20562312"},{"database":"DOI","id":"10.1128/JB.00257-10"}],"title":"Comparative analyses of two thermophilic enzymes exhibiting both beta-1,4 mannosidic and beta-1,4 glucosidic cleavage activities from Caldanaerobius polysaccharolyticus.","publicationDate":"2010","journal":"J. Bacteriol.","firstPage":"4111","lastPage":"4121","volume":"192"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35557.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35557.1"}]},{"referenceNumber":2,"citation":{"id":"24278284","citationType":"journal article","authors":["Oyama T.","Schmitz G.E.","Dodd D.","Han Y.","Burnett A.","Nagasawa N.","Mackie R.I.","Nakamura H.","Morikawa K.","Cann I."],"citationCrossReferences":[{"database":"PubMed","id":"24278284"}],"title":"Mutational and Structural Analyses of Caldanaerobius polysaccharolyticus Man5B Reveal Novel Active Site Residues for Family 5 Glycoside Hydrolases.","publicationDate":"2013","journal":"PLoS ONE","firstPage":"E80448","lastPage":"E80448","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35557.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35557.1"}]},{"referenceNumber":3,"citation":{"id":"25342756","citationType":"journal article","authors":["Chekan J.R.","Kwon I.H.","Agarwal V.","Dodd D.","Revindran V.","Mackie R.I.","Cann I.","Nair S.K."],"citationCrossReferences":[{"database":"PubMed","id":"25342756"},{"database":"DOI","id":"10.1074/jbc.m114.579904"}],"title":"Structural and biochemical basis for mannan utilization by Caldanaerobius polysaccharolyticus strain ATCC BAA-17.","publicationDate":"2014","journal":"J. Biol. Chem.","firstPage":"34965","lastPage":"34977","volume":"289"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH ZN(2+)"],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9F"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"4R9G"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KC180757","properties":[{"key":"ProteinId","value":"AGA35557.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"4R9F","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.40 A"},{"key":"Chains","value":"A=1-447"}]},{"database":"PDB","id":"4R9G","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"A/B=1-447"}]},{"database":"AlphaFoldDB","id":"L0E2M2","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"L0E2M2","properties":[{"key":"Description","value":"-"}]},{"database":"EvolutionaryTrace","id":"L0E2M2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0055052","properties":[{"key":"GoTerm","value":"C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:1901982","properties":[{"key":"GoTerm","value":"F:maltose binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042956","properties":[{"key":"GoTerm","value":"P:maltodextrin transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0015768","properties":[{"key":"GoTerm","value":"P:maltose transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd14748","properties":[{"key":"EntryName","value":"PBP2_UgpB"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.190.10","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR006059","properties":[{"key":"EntryName","value":"SBP"}]},{"database":"PANTHER","id":"PTHR30061","properties":[{"key":"EntryName","value":"MALTOSE-BINDING PERIPLASMIC PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30061:SF50","properties":[{"key":"EntryName","value":"MALTOSE_MALTODEXTRIN-BINDING PERIPLASMIC PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01547","properties":[{"key":"EntryName","value":"SBP_bac_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53850","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKIFLKGKAIIAMLLVIAVLAFAGCSGSSTKNSSTNGNKKQVVLTLWYPWAGPDGDAVVSLAKEYSKTHPNVQIKAQMVSGAGIAATQGGGQGKFLSAVAAGNPPDLVLYWGQDALPGLADQGAIIPLDDYLKDVDTSKFFEAAYNAMKYKGKIYGLPEMVNVRVLFWNKDLFKQAGLDPNTPPKTIAELDQMAAKLTKTKNGTIEQMGFIPWIGQGVPHVMAGVFGTSLVDSNGNPILSPDKNPQLLNLLKWEVSYSDKYGAMNINKFIAGMSQNSSQANDPFVLGKVAMMISGEWQINANKQYNPKLNFGVGPIPQAPGGKPMPSLMDGNTWMIPKGSKHPQEAMDFIKWTMDPQRIADTADKVYNIAPIVEAAKIQKLNNDPYFKEVLNVAQKGSIYYTPAAKGMLSTETAANNAFQAAQYKKSTPEQALKNAQAEAEKSLSQ","length":447,"molWeight":48290,"crc64":"B805BA523AC2EB4A","md5":"9CA61F04F7F287EF26CCDCC44E309E96"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Binding site":7,"Lipidation":2},"uniParcId":"UPI0002A830AE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"D9J0D7","uniProtkbId":"D9J0D7_9THEO","entryAudit":{"firstPublicDate":"2010-10-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2010-10-05","entryVersion":47,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35556.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35556.1"}],"value":"Man5B"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35556.1"}],"value":"man5B"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005641"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361153"}],"value":"Belongs to the glycosyl hydrolase 5 (cellulase A) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"Glycoside hydrolase family 5","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00150"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3W0K"}],"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023001"}],"id":"KW-0136","category":"Biological process","name":"Cellulose degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023295"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361153"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361153"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023326"}],"id":"KW-0624","category":"Biological process","name":"Polysaccharide degradation"}],"references":[{"referenceNumber":1,"citation":{"id":"20562312","citationType":"journal article","authors":["Han Y.","Dodd D.","Hespen C.W.","Ohene-Adjei S.","Schroeder C.M.","Mackie R.I.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"20562312"},{"database":"DOI","id":"10.1128/JB.00257-10"}],"title":"Comparative analyses of two thermophilic enzymes exhibiting both beta-1,4 mannosidic and beta-1,4 glucosidic cleavage activities from Caldanaerobius polysaccharolyticus.","publicationDate":"2010","journal":"J. Bacteriol.","firstPage":"4111","lastPage":"4121","volume":"192"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35556.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35556.1"}]},{"referenceNumber":2,"citation":{"id":"CI-AVKQSJCBO1GVQ","citationType":"submission","authors":["Oyama T.","Schmitz G.E.","Dodd D.","Han Y.","Burnett A.","Nagasawa N.","Mackie R.I.","Nakamura H.","Morikawa K.","Cann I.K.O."],"title":"Crystal structure of a glycoside hydrolase.","publicationDate":"OCT-2012","submissionDatabase":"PDB data bank"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS)"],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3W0K"}]},{"referenceNumber":3,"citation":{"id":"24278284","citationType":"journal article","authors":["Oyama T.","Schmitz G.E.","Dodd D.","Han Y.","Burnett A.","Nagasawa N.","Mackie R.I.","Nakamura H.","Morikawa K.","Cann I."],"citationCrossReferences":[{"database":"PubMed","id":"24278284"}],"title":"Mutational and Structural Analyses of Caldanaerobius polysaccharolyticus Man5B Reveal Novel Active Site Residues for Family 5 Glycoside Hydrolases.","publicationDate":"2013","journal":"PLoS ONE","firstPage":"E80448","lastPage":"E80448","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35556.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35556.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KC180757","properties":[{"key":"ProteinId","value":"AGA35556.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"3W0K","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.60 A"},{"key":"Chains","value":"A/B=1-330"}]},{"database":"AlphaFoldDB","id":"D9J0D7","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"D9J0D7","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH5","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 5"}]},{"database":"EvolutionaryTrace","id":"D9J0D7","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009986","properties":[{"key":"GoTerm","value":"C:cell surface"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008422","properties":[{"key":"GoTerm","value":"F:beta-glucosidase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009251","properties":[{"key":"GoTerm","value":"P:glucan catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR001547","properties":[{"key":"EntryName","value":"Glyco_hydro_5"}]},{"database":"InterPro","id":"IPR050386","properties":[{"key":"EntryName","value":"Glycosyl_hydrolase_5"}]},{"database":"PANTHER","id":"PTHR31297:SF41","properties":[{"key":"EntryName","value":"ENDOGLUCANASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G01830)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31297","properties":[{"key":"EntryName","value":"GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00150","properties":[{"key":"EntryName","value":"Cellulase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKYGFNFQWMYVWEEGREPEPPDKKALDFLAETGFNFVRIPVDYRFWTRNFDYFNPDKKVFEYIDLYLRECSARNIHMCLNLHRAPGYCINRNDIERDNLWLDKRAQDGFVYQWELFAKRYKGVSSKFLSFDLVNEPPNIGQYGLTRENHASLIIRTVEAIRKIDPDREIVIDGLGGGNIAMPELAHLGVVHSGRGYQPMALTHYQASWWDGHKGLPEPYYPDLLWQGKVWNKDTLREYYKPWRDLQQKGVNVHIGEFGCFNKTSNDVAIRWFEDVLSLYKEFEWGYSLWNFKGPFGIVEHGRPGAKYEYYRGFKVDRELLDLLVENRV","length":330,"molWeight":39187,"crc64":"B9B21D9868C52B9D","md5":"3079F06BF8D9EB5D35C0844F35F53DF0"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI0001DE1913"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6QQS3","uniProtkbId":"I6QQS3_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-10-03","entryVersion":40,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44657.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44657.1"}],"value":"Permease"}}]},"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Belongs to the binding protein-dependent transport system permease family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Domain","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"ABC transmembrane type-1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50928"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44657.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44657.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44657.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6QQS3","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0043190","properties":[{"key":"GoTerm","value":"C:ATP-binding cassette (ABC) transporter complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0055085","properties":[{"key":"GoTerm","value":"P:transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06261","properties":[{"key":"EntryName","value":"TM_PBP2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3720.10","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR051393","properties":[{"key":"EntryName","value":"ABC_transporter_permease"}]},{"database":"InterPro","id":"IPR000515","properties":[{"key":"EntryName","value":"MetI-like"}]},{"database":"InterPro","id":"IPR035906","properties":[{"key":"EntryName","value":"MetI-like_sf"}]},{"database":"PANTHER","id":"PTHR30193","properties":[{"key":"EntryName","value":"ABC TRANSPORTER PERMEASE PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30193:SF37","properties":[{"key":"EntryName","value":"INNER MEMBRANE ABC TRANSPORTER PERMEASE PROTEIN YCJO"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00528","properties":[{"key":"EntryName","value":"BPD_transp_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161098","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50928","properties":[{"key":"EntryName","value":"ABC_TM1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEKILSDKKAIFLFVFPAFLVFLVIVLLPIFFSFYYSLLKWDGFSKGVFIGLENYKNLFINNTDGFIISVKNSFILAVLSVFIQLPIALLLALILSRGIKGEKFYRTVYFIPVILSTVVIGQLWMKIYNPNYGLLNFILTKIGLQSLTNQWLGNTKTALGAVFVPILWQYIGYHMLLMYASAKSIPTDIYEAAKIDGATESQIAFRITIPLMKPILKVCVIFAVIGSFKAFDLIYVLTNGGPLHASEVPSTLMYNMIFFRYQYGYGSAMAIFIILESLIGTLIIQKLFGKDVAY","length":294,"molWeight":33205,"crc64":"83576DA5108B4FF2","md5":"C735BE55BC6F2E1ECD27A3AE58F5C744"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":6,"Domain":1},"uniParcId":"UPI0002680B55"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6QTZ7","uniProtkbId":"I6QTZ7_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2025-10-08","lastSequenceUpdateDate":"2012-10-03","entryVersion":43,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44655.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"4: Predicted","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44655.1"}],"value":"Histidine kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44655.1"}],"value":"2.7.13.3"}]}]},"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004370"}],"value":"Membrane","id":"SL-0162"}}]}],"features":[{"type":"Transmembrane","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"HAMP","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50885"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44655.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44655.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44655.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44655.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44655.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6QTZ7","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000155","properties":[{"key":"GoTerm","value":"F:phosphorelay sensor kinase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06225","properties":[{"key":"EntryName","value":"HAMP"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.340.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.565.10","properties":[{"key":"EntryName","value":"Histidine kinase-like ATPase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050640","properties":[{"key":"EntryName","value":"Bact_2-comp_sensor_kinase"}]},{"database":"InterPro","id":"IPR003660","properties":[{"key":"EntryName","value":"HAMP_dom"}]},{"database":"InterPro","id":"IPR036890","properties":[{"key":"EntryName","value":"HATPase_C_sf"}]},{"database":"InterPro","id":"IPR003594","properties":[{"key":"EntryName","value":"HATPase_dom"}]},{"database":"InterPro","id":"IPR010559","properties":[{"key":"EntryName","value":"Sig_transdc_His_kin_internal"}]},{"database":"PANTHER","id":"PTHR34220","properties":[{"key":"EntryName","value":"SENSOR HISTIDINE KINASE YPDA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34220:SF7","properties":[{"key":"EntryName","value":"SENSOR HISTIDINE KINASE YPDA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02518","properties":[{"key":"EntryName","value":"HATPase_c"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06580","properties":[{"key":"EntryName","value":"His_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00304","properties":[{"key":"EntryName","value":"HAMP"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55874","properties":[{"key":"EntryName","value":"ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF158472","properties":[{"key":"EntryName","value":"HAMP domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50885","properties":[{"key":"EntryName","value":"HAMP"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIQSTNWYNRLLNLNGGYILEVNAGGLLENNKDNQGYISFIRVINDINTQKPSGIMIINISKLYLSKYINSAINTYTSSIILKDEKGNSIIEPTNISKNLNNKIFNYIRPNGSTIKNINGEVYIISHIENEFGWNIISITPFNELNSQFWIYNIILLFVIIINVILLILGLLFISLFITQPIIKLVNSMKGIKDGKFEKVNIITGNDEIGMLKDVYNKMIDEIKKLISDIINEQKIKRKLELEVMQSQIKPHFLFNSFDAISALILMGDTKNASKIVKALGKFYRSFLINGEEITIKEELDIINSYLTIQKIRFGDKFNVEKDIDERTLSYKIPKLILQPLVENALNHGIRSKDGQGIISIKALHGDNQIKLIVEDNGKGMSEEKIKEIECGKSKVLALDPQ","length":402,"molWeight":45715,"crc64":"CCBB02E90CF2F829","md5":"A3FA3F3EEED79E8553872533AFC8A8A9"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1},"countByFeatureType":{"Transmembrane":1,"Domain":1},"uniParcId":"UPI0002680B52"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6R6X6","uniProtkbId":"I6R6X6_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-10-03","entryVersion":33,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44649.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44649.1"}],"value":"Xyl3A"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44649.1"}],"value":"3.2.1.37"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44649.1"}],"value":"xyl3A"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005336"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361161"}],"value":"Belongs to the glycosyl hydrolase 3 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":689,"modifier":"EXACT"},"end":{"value":758,"modifier":"EXACT"}},"description":"Fibronectin type III-like","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01217"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361161"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44649.1"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361161"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44649.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44649.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44649.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6R6X6","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"I6R6X6","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH3","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 3"}]},{"database":"GO","id":"GO:0008422","properties":[{"key":"GoTerm","value":"F:beta-glucosidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0009044","properties":[{"key":"GoTerm","value":"F:xylan 1,4-beta-xylosidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009251","properties":[{"key":"GoTerm","value":"P:glucan catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"3.20.20.300:FF:000011","properties":[{"key":"EntryName","value":"Glycosyl hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.40.10:FF:000495","properties":[{"key":"EntryName","value":"Periplasmic beta-glucosidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1700","properties":[{"key":"EntryName","value":"Glycoside hydrolase family 3 C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.300","properties":[{"key":"EntryName","value":"Glycoside hydrolase, family 3, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.10","properties":[{"key":"EntryName","value":"Immunoglobulins"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR051915","properties":[{"key":"EntryName","value":"Cellulose_Degrad_GH3"}]},{"database":"InterPro","id":"IPR026891","properties":[{"key":"EntryName","value":"Fn3-like"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR019800","properties":[{"key":"EntryName","value":"Glyco_hydro_3_AS"}]},{"database":"InterPro","id":"IPR002772","properties":[{"key":"EntryName","value":"Glyco_hydro_3_C"}]},{"database":"InterPro","id":"IPR036881","properties":[{"key":"EntryName","value":"Glyco_hydro_3_C_sf"}]},{"database":"InterPro","id":"IPR001764","properties":[{"key":"EntryName","value":"Glyco_hydro_3_N"}]},{"database":"InterPro","id":"IPR036962","properties":[{"key":"EntryName","value":"Glyco_hydro_3_N_sf"}]},{"database":"InterPro","id":"IPR013783","properties":[{"key":"EntryName","value":"Ig-like_fold"}]},{"database":"PANTHER","id":"PTHR30620:SF123","properties":[{"key":"EntryName","value":"BETA-XYLOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30620","properties":[{"key":"EntryName","value":"PERIPLASMIC BETA-GLUCOSIDASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14310","properties":[{"key":"EntryName","value":"Fn3-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00933","properties":[{"key":"EntryName","value":"Glyco_hydro_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01915","properties":[{"key":"EntryName","value":"Glyco_hydro_3_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00133","properties":[{"key":"EntryName","value":"GLHYDRLASE3"}]},{"database":"SMART","id":"SM01217","properties":[{"key":"EntryName","value":"Fn3_like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52279","properties":[{"key":"EntryName","value":"Beta-D-glucan exohydrolase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00775","properties":[{"key":"EntryName","value":"GLYCOSYL_HYDROL_F3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKGNSKESALYLDATQPVEKRVEDLLSRMTLDEKIAQLSSVWVYELLDNMEFSVDKAKDLLKDGIGQITRIGGASNLGPKESAQLANEIQRYLIENTRLGIPALVHEESCSGYMAKGATCFPQTIGVASTWNTELVKQMGSVIREQMKAVGAHQALAPLMDVARDARWGRVEETFGEDPYLISEMGVSYIEGLQGGNIKDGIMATVKHFVGYGFSEGGMNWAPAHIPERELREVFLLPFEAAVKKAKTASVMAAYHELDGIPCHGSKKLLTQILRNEWGFDGLVVSDYFGVNMLYEYHHVARDKGEAAKIALQAGVDIELPSRDCYGQPLKEAVQKGLVEEALIDEVVRRILRMKFLSGVFENPYVDVEKAAEVFDTPDQRKLAYKLAQQSIVLLKNQGDLLPLKKDIKSIAVIGPNADSVRNIIGDYAYPCHIESLVETKEQSNVFNTPVPDKVSLVDNFVPIKSILEGIKGKISPETELHYAKGCEVTGDDKGGFAEAIEAAKKSDVAIVVVGDKAGLTDDCTSGESRDRADLNLPGVQQELVEAIYNTGTPTVVVLVNGRPLSINWISRHIPAIIEAWLPGEEGAAAVADVLFGDYNPGGKLPVSFPRSVGQVPVYYNHKPSGGRSHWKGDYVEMSTKPLYPFGYGLSYTKFEFSNLEIAPSEVYDDGKVRISVDVQNAGKLEGDEVVQLYVRNEVSNVTRPVKELKGFKRVSLRPGEKKKVVFELSVSQLGFYDEDMRYVVQPGTVKVMIGSSSEDIKVAGEFKVTGKTVQVGESKEFFTKVEVV","length":789,"molWeight":86760,"crc64":"B821546C0F398F61","md5":"3D83C9CE80A67CBBE435A752F2A5A9EF"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI0002680B4E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6R6Y3","uniProtkbId":"I6R6Y3_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2012-10-03","entryVersion":22,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44659.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"4: Predicted","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44659.1"}],"value":"Polysaccharide deacetylase"}}]},"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004613"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01014"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"NodB homology","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51677"}]},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01014"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01014"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01014"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01014"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44659.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44659.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44659.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6R6Y3","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0016810","properties":[{"key":"GoTerm","value":"F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd10967","properties":[{"key":"EntryName","value":"CE4_GLA_like_6s"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.370","properties":[{"key":"EntryName","value":"Glycoside hydrolase/deacetylase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011330","properties":[{"key":"EntryName","value":"Glyco_hydro/deAcase_b/a-brl"}]},{"database":"InterPro","id":"IPR002509","properties":[{"key":"EntryName","value":"NODB_dom"}]},{"database":"PANTHER","id":"PTHR34216","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34216:SF3","properties":[{"key":"EntryName","value":"POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01522","properties":[{"key":"EntryName","value":"Polysacc_deac_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88713","properties":[{"key":"EntryName","value":"Glycoside hydrolase/deacetylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51677","properties":[{"key":"EntryName","value":"NODB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKISFGYYHGGKKKALTMSYDDGQVFDRRLVEIFNKYGIKGTFNLNSGRFDTEPYVSKKEIKELYKGHEVAVHSLNHPCLSLIPPEELAYQIMEDRKNLESLVGYQVRGMAYPYGDYSDALLNSLTSFGIEYSRTVKSTKSFGIPNNFLEWHPTCHHDQDVIQKLKEFKNLKEWEQMPLFYVWGHSFEFDRNGNWDLIEEFCKMASFDETVWYATNIEIKDYIDALRSLKFSADRSMVYNPSAIPVWIGVDGEPIKIDSGERIKLK","length":266,"molWeight":30967,"crc64":"0CBAF8B8BB15DD4F","md5":"E30A65B2DA6EE752A62699776E1D5B5D"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":3},"uniParcId":"UPI0002680B57"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6RCT7","uniProtkbId":"I6RCT7_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-10-03","entryVersion":14,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44648.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"4: Predicted","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44648.1"}],"value":"Uncharacterized protein"}}]},"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44648.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44648.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44648.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6RCT7","properties":[{"key":"Description","value":"-"}]}],"sequence":{"value":"MNRVESSTHYTYSLHFALLCVSPFDLYILYHKIAKRASVMKYLGKKKRKEEET","length":53,"molWeight":6325,"crc64":"CDE9937654D6C05F","md5":"077B9C09CD93C1C41A95C76D91A031BD"},"extraAttributes":{"uniParcId":"UPI0002680B4C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6RCU3","uniProtkbId":"I6RCU3_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-10-03","entryVersion":36,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44658.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44658.1"}],"value":"ATP-binding protein"}}]},"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Belongs to the binding protein-dependent transport system permease family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Domain","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"ABC transmembrane type-1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50928"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44658.1"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44658.1"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44658.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44658.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44658.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6RCU3","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0043190","properties":[{"key":"GoTerm","value":"C:ATP-binding cassette (ABC) transporter complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0055085","properties":[{"key":"GoTerm","value":"P:transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06261","properties":[{"key":"EntryName","value":"TM_PBP2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3720.10","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000515","properties":[{"key":"EntryName","value":"MetI-like"}]},{"database":"InterPro","id":"IPR035906","properties":[{"key":"EntryName","value":"MetI-like_sf"}]},{"database":"PANTHER","id":"PTHR43744","properties":[{"key":"EntryName","value":"ABC TRANSPORTER PERMEASE PROTEIN MG189-RELATED-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43744:SF8","properties":[{"key":"EntryName","value":"SN-GLYCEROL-3-PHOSPHATE TRANSPORT SYSTEM PERMEASE PROTEIN UGPE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00528","properties":[{"key":"EntryName","value":"BPD_transp_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161098","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50928","properties":[{"key":"EntryName","value":"ABC_TM1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MENIAGENKKSWFKKIGFYVLEAILVIWAIVQIYPLFWLFLFSVKNNTEIFGGNILGFPRIWQWSNYAVALSSGNVGKYFINSTIVTVLTIIISSILVATSAYAIVRMKWKYSKLVLTIFLTGMMVPLHATLLPLFIILKNLNLLNTYASLVIPYVAFAIPMGIFILTGFLYTIPRELEESAFLDGCSIYKSFYYVILPLIRPALATIAIFTYLSTWNELMFANTFINDDAIKTLTVGIMSLSGQYQTEWGPIGAGLVIATIPTILIYVLLSEQVQKSLVVGAIKG","length":286,"molWeight":32018,"crc64":"27EAFA6BD6D1FE97","md5":"76FAFF18292AE5841820B744FEEFC9A0"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":6,"Domain":1},"uniParcId":"UPI0002680B56"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6RGT3","uniProtkbId":"I6RGT3_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2012-10-03","entryVersion":31,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44651.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"4: Predicted","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44651.1"}],"value":"XylI"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44651.1"}],"value":"5.3.1.5"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44651.1"}],"value":"xylI"}}],"features":[{"type":"Domain","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"Xylose isomerase-like TIM barrel","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01261"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44651.1"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"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"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44651.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44651.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44651.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6RGT3","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0008740","properties":[{"key":"GoTerm","value":"F:L-rhamnose isomerase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009045","properties":[{"key":"GoTerm","value":"F:xylose isomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0019324","properties":[{"key":"GoTerm","value":"P:L-lyxose metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019301","properties":[{"key":"GoTerm","value":"P:rhamnose catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.20.20.150","properties":[{"key":"EntryName","value":"Divalent-metal-dependent TIM barrel enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050337","properties":[{"key":"EntryName","value":"L-rhamnose_isomerase"}]},{"database":"InterPro","id":"IPR036237","properties":[{"key":"EntryName","value":"Xyl_isomerase-like_sf"}]},{"database":"InterPro","id":"IPR013022","properties":[{"key":"EntryName","value":"Xyl_isomerase-like_TIM-brl"}]},{"database":"PANTHER","id":"PTHR30268","properties":[{"key":"EntryName","value":"L-RHAMNOSE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30268:SF0","properties":[{"key":"EntryName","value":"L-RHAMNOSE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01261","properties":[{"key":"EntryName","value":"AP_endonuc_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51658","properties":[{"key":"EntryName","value":"Xylose isomerase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFDVRDQKVRRSPDEVLEHLKNFHLDLKFSVGIWYFSPSGSRFKEAASAPRSIEERLDIIASLKDYGVSALEAHYPNEINENNLDTYKKFSKDTGIRILTVIPNLFYQKQWEFSSLASPIDEVRNKAIERLKISLQLNKELNTDFAIVWHGGDGYENPFGIDFMAMRDRFAYGIAEAMDQVPGVRVAIEPKPYEPRGRIIYGTTAEGILVAQKVEGALKNEENKRILSEGHSLVGLNPEVGHVLMAYEDLPYAFSLAMEYGKLLHTHWNSQPAGNYDQDQNVGVISPEQAEAALYVLKMHGYKGYFGIDINPERMPVEVAVKNNIDAIRSMNARIEELDHEAIVEAVNNPDKHRGLIEAILIRARAPKTISLPPISSVIK","length":380,"molWeight":42923,"crc64":"075EDFD4404D2EC5","md5":"2408C834AB46169DF0A03E4AAF12B13E"},"extraAttributes":{"countByFeatureType":{"Domain":1},"uniParcId":"UPI0002680B4F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"I6RGT7","uniProtkbId":"I6RGT7_9THEO","entryAudit":{"firstPublicDate":"2012-10-03","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2012-10-03","entryVersion":21,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44656.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"4: Predicted","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44656.1"}],"value":"Xbp1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44656.1"}],"value":"xbp1"}}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5038979407"},{"type":"Lipidation","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0564","category":"PTM","name":"Palmitate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"22918832","citationType":"journal article","authors":["Han Y.","Agarwal V.","Dodd D.","Kim J.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"22918832"},{"database":"DOI","id":"10.1074/jbc.M112.391532"}],"title":"Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.","publicationDate":"2012","journal":"J. Biol. Chem.","firstPage":"34946","lastPage":"34960","volume":"287"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44656.1"}],"value":"KMCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AFM44656.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JX087428","properties":[{"key":"ProteinId","value":"AFM44656.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"I6RGT7","properties":[{"key":"Description","value":"-"}]},{"database":"CDD","id":"cd14749","properties":[{"key":"EntryName","value":"PBP2_XBP1_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.190.10","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR050490","properties":[{"key":"EntryName","value":"Bact_solute-bd_prot1"}]},{"database":"InterPro","id":"IPR006059","properties":[{"key":"EntryName","value":"SBP"}]},{"database":"PANTHER","id":"PTHR43649","properties":[{"key":"EntryName","value":"ARABINOSE-BINDING PROTEIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43649:SF14","properties":[{"key":"EntryName","value":"BLR3389 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01547","properties":[{"key":"EntryName","value":"SBP_bac_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53850","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKGFKKLMLIVLSLLLVLSASACSSNNLSKSNTSNSSKTSSSSKKITLTFWNLFTGEPAKTKVKEIIDQWNKENPNVQIVESVTENDAYKTKIKAAIAANEAPDIFQTWAGGFSQPFVEAGKVLQLDSYLNDGTKDQLLPGSFDNVTYNGKIYGIPFDQQASVLYINKELFDKYNVKVPTTFSELIDAIKTFKSKGVTPFALGEKDEWPGMWYYDMIALREGGVQLTRDALNGKASFDNQAFTDAAQKLQDMVNAGAFDSGFMGLTRDEATAEFNQGKAAMYFGGNFDAAAFVSDPSSLVKGKIEAVRFPTIEGGKGDPTEYIGGTVGALMVSANSKYKDEAVRAAKYLAKQLSDMDYLIATGLPAWKYDNIDQSKVDPLEIQIMNNIVANAKGSVPAWDIYLSGDAAQTHKDLVAQLFAKQITPEEYSKQMQQKINGK","length":439,"molWeight":48102,"crc64":"923B0B65AFA33F66","md5":"9B1210BB738880870CB8C373AB851DB9"},"extraAttributes":{"countByFeatureType":{"Signal":1,"Chain":1,"Lipidation":2},"uniParcId":"UPI0002680B54"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"L0E134","uniProtkbId":"L0E134_9THEO","entryAudit":{"firstPublicDate":"2013-03-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-03-06","entryVersion":45,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35558.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"4: Predicted","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35558.1"}],"value":"ManR"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35558.1"}],"value":"manR"}}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"HTH lacI-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50932"}]},{"type":"DNA binding","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"H-T-H motif","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00111"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00111"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022491"}],"id":"KW-0678","category":"Molecular function","name":"Repressor"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00111"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00111"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"}],"references":[{"referenceNumber":1,"citation":{"id":"20562312","citationType":"journal article","authors":["Han Y.","Dodd D.","Hespen C.W.","Ohene-Adjei S.","Schroeder C.M.","Mackie R.I.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"20562312"},{"database":"DOI","id":"10.1128/JB.00257-10"}],"title":"Comparative analyses of two thermophilic enzymes exhibiting both beta-1,4 mannosidic and beta-1,4 glucosidic cleavage activities from Caldanaerobius polysaccharolyticus.","publicationDate":"2010","journal":"J. Bacteriol.","firstPage":"4111","lastPage":"4121","volume":"192"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35558.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35558.1"}]},{"referenceNumber":2,"citation":{"id":"24278284","citationType":"journal article","authors":["Oyama T.","Schmitz G.E.","Dodd D.","Han Y.","Burnett A.","Nagasawa N.","Mackie R.I.","Nakamura H.","Morikawa K.","Cann I."],"citationCrossReferences":[{"database":"PubMed","id":"24278284"}],"title":"Mutational and Structural Analyses of Caldanaerobius polysaccharolyticus Man5B Reveal Novel Active Site Residues for Family 5 Glycoside Hydrolases.","publicationDate":"2013","journal":"PLoS ONE","firstPage":"E80448","lastPage":"E80448","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35558.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35558.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KC180757","properties":[{"key":"ProteinId","value":"AGA35558.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"L0E134","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0003700","properties":[{"key":"GoTerm","value":"F:DNA-binding transcription factor activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000976","properties":[{"key":"GoTerm","value":"F:transcription cis-regulatory region binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01392","properties":[{"key":"EntryName","value":"HTH_LacI"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd19974","properties":[{"key":"EntryName","value":"PBP1_LacI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2300","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.260.40","properties":[{"key":"EntryName","value":"lambda repressor-like DNA-binding domains"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000843","properties":[{"key":"EntryName","value":"HTH_LacI"}]},{"database":"InterPro","id":"IPR046335","properties":[{"key":"EntryName","value":"LacI/GalR-like_sensor"}]},{"database":"InterPro","id":"IPR010982","properties":[{"key":"EntryName","value":"Lambda_DNA-bd_dom_sf"}]},{"database":"InterPro","id":"IPR028082","properties":[{"key":"EntryName","value":"Peripla_BP_I"}]},{"database":"PANTHER","id":"PTHR30146:SF148","properties":[{"key":"EntryName","value":"HTH-TYPE TRANSCRIPTIONAL REPRESSOR PURR-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30146","properties":[{"key":"EntryName","value":"LACI-RELATED TRANSCRIPTIONAL REPRESSOR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00356","properties":[{"key":"EntryName","value":"LacI"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13377","properties":[{"key":"EntryName","value":"Peripla_BP_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00354","properties":[{"key":"EntryName","value":"HTH_LACI"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47413","properties":[{"key":"EntryName","value":"lambda repressor-like DNA-binding domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53822","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like I"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00356","properties":[{"key":"EntryName","value":"HTH_LACI_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50932","properties":[{"key":"EntryName","value":"HTH_LACI_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGRVRLEDIAAVVGVSKNTVSKALRGAGGVSAEMREKIRETALKMGYRRVRDLDKEVENITVLCRESFFGEPTFWSSILYGIENSARNRNIKLSVTAVDAEDEENLNIPYAINKETTNGIIIVGTLNDGFIKKIKALGIPIVVIDHYSEEIQCDYINSANKKGIYEALKYLYKSGHRKIGFIGNNEWAYSFRERYESFIYYAKKFNIEVDEDYIWLDISLKRTDFIEDTDYFKRKIKYSEKFPSAWICSNDKIALAFIKSLMDLGISVPDKVSVIGFDDIEIARISHPRLTTLNVPKQAMGERAVSQLLFRISNEDKPYEYIELNTSLIVRDSTKGVF","length":338,"molWeight":38661,"crc64":"E2A66A8BA1AEDB8A","md5":"040850EF9062026C92ED324ED3F06D1D"},"extraAttributes":{"countByFeatureType":{"Domain":1,"DNA binding":1},"uniParcId":"UPI0002A7BE34"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"L0E2R8","uniProtkbId":"L0E2R8_9THEO","entryAudit":{"firstPublicDate":"2013-03-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2013-03-06","entryVersion":25,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35561.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35561.1"}],"value":"Glycoside hydrolase family 43"}}],"flag":"Fragment"},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024356"}],"value":"Belongs to the glycosyl hydrolase 130 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Non-terminal residue","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35561.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35561.1"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"20562312","citationType":"journal article","authors":["Han Y.","Dodd D.","Hespen C.W.","Ohene-Adjei S.","Schroeder C.M.","Mackie R.I.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"20562312"},{"database":"DOI","id":"10.1128/JB.00257-10"}],"title":"Comparative analyses of two thermophilic enzymes exhibiting both beta-1,4 mannosidic and beta-1,4 glucosidic cleavage activities from Caldanaerobius polysaccharolyticus.","publicationDate":"2010","journal":"J. Bacteriol.","firstPage":"4111","lastPage":"4121","volume":"192"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35561.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35561.1"}]},{"referenceNumber":2,"citation":{"id":"24278284","citationType":"journal article","authors":["Oyama T.","Schmitz G.E.","Dodd D.","Han Y.","Burnett A.","Nagasawa N.","Mackie R.I.","Nakamura H.","Morikawa K.","Cann I."],"citationCrossReferences":[{"database":"PubMed","id":"24278284"}],"title":"Mutational and Structural Analyses of Caldanaerobius polysaccharolyticus Man5B Reveal Novel Active Site Residues for Family 5 Glycoside Hydrolases.","publicationDate":"2013","journal":"PLoS ONE","firstPage":"E80448","lastPage":"E80448","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35561.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35561.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KC180757","properties":[{"key":"ProteinId","value":"AGA35561.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"L0E2R8","properties":[{"key":"Description","value":"-"}]},{"database":"Gene3D","id":"2.115.10.20","properties":[{"key":"EntryName","value":"Glycosyl hydrolase domain, family 43"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023296","properties":[{"key":"EntryName","value":"Glyco_hydro_beta-prop_sf"}]},{"database":"InterPro","id":"IPR007184","properties":[{"key":"EntryName","value":"Mannoside_phosphorylase"}]},{"database":"PANTHER","id":"PTHR34106:SF1","properties":[{"key":"EntryName","value":"1,4-BETA-MANNOSYL-N-ACETYLGLUCOSAMINE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34106","properties":[{"key":"EntryName","value":"GLYCOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04041","properties":[{"key":"EntryName","value":"Glyco_hydro_130"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF75005","properties":[{"key":"EntryName","value":"Arabinanase/levansucrase/invertase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKQLIVGEALPNIPWQDRPAGCNDVVWRYQQNPVIPRDLIPSSNSIFNSAVVPFNGEFAGVFRCDTKSRQMEIHSGRSKDGIHWEIDHERIKFICDDEEVSRFVYAYDPRVCKIEDRYYITWCNGYHGYPTIGVAYTYDFKEFYQMENAFLPFNRNGVLFPRKIKGKYAMLSRPSDNGHTPFGDIFYSESPDMVHWGHHRHVMSPNKPWESTKIGAGPV","length":220,"molWeight":25532,"crc64":"939E83A12E271C64","md5":"6D42CC5AD914582B2502443406B438CB"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Non-terminal residue":1},"uniParcId":"UPI0002A8710B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"L0E2W7","uniProtkbId":"L0E2W7_9THEO","entryAudit":{"firstPublicDate":"2013-03-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-03-06","entryVersion":38,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35559.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35559.1"}],"value":"Permease"}}]},"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Belongs to the binding protein-dependent transport system permease family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Domain","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"ABC transmembrane type-1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50928"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"20562312","citationType":"journal article","authors":["Han Y.","Dodd D.","Hespen C.W.","Ohene-Adjei S.","Schroeder C.M.","Mackie R.I.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"20562312"},{"database":"DOI","id":"10.1128/JB.00257-10"}],"title":"Comparative analyses of two thermophilic enzymes exhibiting both beta-1,4 mannosidic and beta-1,4 glucosidic cleavage activities from Caldanaerobius polysaccharolyticus.","publicationDate":"2010","journal":"J. Bacteriol.","firstPage":"4111","lastPage":"4121","volume":"192"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35559.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35559.1"}]},{"referenceNumber":2,"citation":{"id":"24278284","citationType":"journal article","authors":["Oyama T.","Schmitz G.E.","Dodd D.","Han Y.","Burnett A.","Nagasawa N.","Mackie R.I.","Nakamura H.","Morikawa K.","Cann I."],"citationCrossReferences":[{"database":"PubMed","id":"24278284"}],"title":"Mutational and Structural Analyses of Caldanaerobius polysaccharolyticus Man5B Reveal Novel Active Site Residues for Family 5 Glycoside Hydrolases.","publicationDate":"2013","journal":"PLoS ONE","firstPage":"E80448","lastPage":"E80448","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35559.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35559.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KC180757","properties":[{"key":"ProteinId","value":"AGA35559.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"L0E2W7","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0043190","properties":[{"key":"GoTerm","value":"C:ATP-binding cassette (ABC) transporter complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0055085","properties":[{"key":"GoTerm","value":"P:transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06261","properties":[{"key":"EntryName","value":"TM_PBP2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3720.10","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR051393","properties":[{"key":"EntryName","value":"ABC_transporter_permease"}]},{"database":"InterPro","id":"IPR000515","properties":[{"key":"EntryName","value":"MetI-like"}]},{"database":"InterPro","id":"IPR035906","properties":[{"key":"EntryName","value":"MetI-like_sf"}]},{"database":"PANTHER","id":"PTHR30193","properties":[{"key":"EntryName","value":"ABC TRANSPORTER PERMEASE PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30193:SF1","properties":[{"key":"EntryName","value":"ABC TRANSPORTER PERMEASE PROTEIN YESP-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00528","properties":[{"key":"EntryName","value":"BPD_transp_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161098","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50928","properties":[{"key":"EntryName","value":"ABC_TM1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGAVKRGKRMSLEREEAIKGVLFISPWIIGFLVFTLYPFISSFYYSFTRFGGIGTPVFIGLKNYVNLFHDKLFYLSLYNTLYYTVIAVPLGVVLGIAVALLLNQKIRGLSFFRTIIYMPYMVPTVASAILWMWILDPQFGLINSLLASIGIKGPGWLADPAWSKMSLIIMAQWGMGQAVVIYLSGLRNVPTELYESADIDGANIFQKFFHVTLPMMSPVILYNVILGVINSLQYFTQAYIMTSGGPVNSTLFYSLYLFRESFMNYHMGYASAMAWILLVIIAACVYLLFKTSAKYVYYSGE","length":301,"molWeight":33997,"crc64":"C2515CB3C4EFC49C","md5":"025A7C7393460DCAF2F36045B87B558C"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":5,"Domain":1},"uniParcId":"UPI0002A7C04E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"L0E4E2","uniProtkbId":"L0E4E2_9THEO","entryAudit":{"firstPublicDate":"2013-03-06","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-03-06","entryVersion":37,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35560.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35560.1"}],"value":"Permease"}}]},"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"value":"Belongs to the binding protein-dependent transport system permease family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Transmembrane","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}]},{"type":"Domain","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"ABC transmembrane type-1","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50928"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00441"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363032"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"20562312","citationType":"journal article","authors":["Han Y.","Dodd D.","Hespen C.W.","Ohene-Adjei S.","Schroeder C.M.","Mackie R.I.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"20562312"},{"database":"DOI","id":"10.1128/JB.00257-10"}],"title":"Comparative analyses of two thermophilic enzymes exhibiting both beta-1,4 mannosidic and beta-1,4 glucosidic cleavage activities from Caldanaerobius polysaccharolyticus.","publicationDate":"2010","journal":"J. Bacteriol.","firstPage":"4111","lastPage":"4121","volume":"192"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35560.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35560.1"}]},{"referenceNumber":2,"citation":{"id":"24278284","citationType":"journal article","authors":["Oyama T.","Schmitz G.E.","Dodd D.","Han Y.","Burnett A.","Nagasawa N.","Mackie R.I.","Nakamura H.","Morikawa K.","Cann I."],"citationCrossReferences":[{"database":"PubMed","id":"24278284"}],"title":"Mutational and Structural Analyses of Caldanaerobius polysaccharolyticus Man5B Reveal Novel Active Site Residues for Family 5 Glycoside Hydrolases.","publicationDate":"2013","journal":"PLoS ONE","firstPage":"E80448","lastPage":"E80448","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35560.1"}],"value":"KMTHCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AGA35560.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KC180757","properties":[{"key":"ProteinId","value":"AGA35560.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"L0E4E2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0043190","properties":[{"key":"GoTerm","value":"C:ATP-binding cassette (ABC) transporter complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0055085","properties":[{"key":"GoTerm","value":"P:transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06261","properties":[{"key":"EntryName","value":"TM_PBP2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3720.10","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000515","properties":[{"key":"EntryName","value":"MetI-like"}]},{"database":"InterPro","id":"IPR035906","properties":[{"key":"EntryName","value":"MetI-like_sf"}]},{"database":"PANTHER","id":"PTHR43744","properties":[{"key":"EntryName","value":"ABC TRANSPORTER PERMEASE PROTEIN MG189-RELATED-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43744:SF8","properties":[{"key":"EntryName","value":"SN-GLYCEROL-3-PHOSPHATE TRANSPORT SYSTEM PERMEASE PROTEIN UGPE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00528","properties":[{"key":"EntryName","value":"BPD_transp_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161098","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50928","properties":[{"key":"EntryName","value":"ABC_TM1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIVKKSTMDLIGRIIVYALLIVVSVLFLLPFLWMVSTALKPIDKIFTIPPQFIPQTFMWQNFTDAINAIPFWTYLSNTLIYAVFSMLGTVLSSTVIAYGFSRLRWKGRDTVFFIVLMTMMLPYQVTMIPLFIIFKNLGFINTLLPLIVPSFFGVPFYIFLIRQFMMSIPKEMSEAARIDGASEWGILWRIIVPITKPALWTVAIFQMIAAWQDFLGPLIYLSDESKYTMSLGLQQFQTAHGAIWNQLMAVSLIMTIPMIVLFFITQKALLEGLTLTGSIKA","length":281,"molWeight":32073,"crc64":"5EBA9A262F76977D","md5":"5F7C431D2496B50BE07C0CC299FD56EF"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":6,"Domain":1},"uniParcId":"UPI0002A81A73"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q9ZA17","uniProtkbId":"Q9ZA17_9THEO","entryAudit":{"firstPublicDate":"1999-05-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1999-05-01","entryVersion":124,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Caldanaerobius polysaccharolyticus","taxonId":44256,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD09354.1"}],"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Thermoanaerobacterales","Thermoanaerobacteraceae","Caldanaerobius"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD09354.1"}],"value":"S-layer associated multidomain endoglucanase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD09354.1"}],"value":"celA"}}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":1097,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5054102814"},{"type":"Domain","location":{"start":{"value":908,"modifier":"EXACT"},"end":{"value":971,"modifier":"EXACT"}},"description":"SLH","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51272"}]},{"type":"Domain","location":{"start":{"value":972,"modifier":"EXACT"},"end":{"value":1031,"modifier":"EXACT"}},"description":"SLH","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51272"}]},{"type":"Domain","location":{"start":{"value":1038,"modifier":"EXACT"},"end":{"value":1097,"modifier":"EXACT"}},"description":"SLH","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51272"}]},{"type":"Binding site","location":{"start":{"value":621,"modifier":"EXACT"},"end":{"value":621,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3OEB"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":623,"modifier":"EXACT"},"end":{"value":623,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEY"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":645,"modifier":"EXACT"},"end":{"value":645,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEW"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEX"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":648,"modifier":"EXACT"},"end":{"value":648,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEW"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEX"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":749,"modifier":"EXACT"},"end":{"value":749,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEW"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEX"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":764,"modifier":"EXACT"},"end":{"value":764,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEZ"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}},{"type":"Binding site","location":{"start":{"value":766,"modifier":"EXACT"},"end":{"value":766,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEZ"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}},{"type":"Binding site","location":{"start":{"value":788,"modifier":"EXACT"},"end":{"value":788,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEZ"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}},{"type":"Binding site","location":{"start":{"value":791,"modifier":"EXACT"},"end":{"value":791,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEZ"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}},{"type":"Binding site","location":{"start":{"value":892,"modifier":"EXACT"},"end":{"value":892,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEZ"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEW"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEX"}],"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEW"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEX"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023295"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEW"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEX"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4CUS9VABDBQTE","citationType":"submission","authors":["Hofemeister J.W."],"publicationDate":"DEC-1996","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD09354.1"}],"value":"KM-THCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD09354.1"}]},{"referenceNumber":2,"citation":{"id":"10049399","citationType":"journal article","authors":["Cann I.K.","Kocherginskaya S.","King M.R.","White B.A.","Mackie R.I."],"citationCrossReferences":[{"database":"PubMed","id":"10049399"}],"title":"Molecular cloning, sequencing, and expression of a novel multidomain mannanase gene from Thermoanaerobacterium polysaccharolyticum.","publicationDate":"1999","journal":"J. Bacteriol.","firstPage":"1643","lastPage":"1651","volume":"181"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD09354.1"}],"value":"KM-THCJ","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD09354.1"}]},{"referenceNumber":3,"citation":{"id":"18025086","citationType":"journal article","authors":["Bae B.","Ohene-Adjei S.","Kocherginskaya S.","Mackie R.I.","Spies M.A.","Cann I.K.","Nair S.K."],"citationCrossReferences":[{"database":"PubMed","id":"18025086"},{"database":"DOI","id":"10.1074/jbc.m706513200"}],"title":"Molecular basis for the selectivity and specificity of ligand recognition by the family 16 carbohydrate-binding modules from Thermoanaerobacterium polysaccharolyticum ManA.","publicationDate":"2008","journal":"J. Biol. Chem.","firstPage":"12415","lastPage":"12425","volume":"283"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 614-756 IN COMPLEX WITH CA(2+)"],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEW"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"2ZEX"}]},{"referenceNumber":4,"citation":{"id":"20739280","citationType":"journal article","authors":["Su X.","Agarwal V.","Dodd D.","Bae B.","Mackie R.I.","Nair S.K.","Cann I.K."],"citationCrossReferences":[{"database":"PubMed","id":"20739280"},{"database":"DOI","id":"10.1074/jbc.m110.168302"}],"title":"Mutational insights into the roles of amino acid residues in ligand binding for two closely related family 16 carbohydrate binding modules.","publicationDate":"2010","journal":"J. Biol. Chem.","firstPage":"34665","lastPage":"34676","volume":"285"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 614-756 IN COMPLEX WITH CA(2+)"],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3OEA"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"3OEB"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U82255","properties":[{"key":"ProteinId","value":"AAD09354.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"2ZEW","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.40 A"},{"key":"Chains","value":"A/B=614-756"}]},{"database":"PDB","id":"2ZEX","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.20 A"},{"key":"Chains","value":"A/B=614-756"}]},{"database":"PDB","id":"2ZEY","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"A/B=614-756"}]},{"database":"PDB","id":"2ZEZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A/B/C/D=756-899"}]},{"database":"PDB","id":"3OEA","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.35 A"},{"key":"Chains","value":"A/B=614-756"}]},{"database":"PDB","id":"3OEB","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.55 A"},{"key":"Chains","value":"A=614-756"}]},{"database":"AlphaFoldDB","id":"Q9ZA17","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"Q9ZA17","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9ZA17","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"CBM16","properties":[{"key":"FamilyName","value":"Carbohydrate-Binding Module Family 16"}]},{"database":"CAZy","id":"GH5","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 5"}]},{"database":"EvolutionaryTrace","id":"Q9ZA17","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0004553","properties":[{"key":"GoTerm","value":"F:hydrolase activity, hydrolyzing O-glycosyl compounds"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000272","properties":[{"key":"GoTerm","value":"P:polysaccharide catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"2.60.120.260","properties":[{"key":"EntryName","value":"Galactose-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.10","properties":[{"key":"EntryName","value":"Immunoglobulins"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR003305","properties":[{"key":"EntryName","value":"CenC_carb-bd"}]},{"database":"InterPro","id":"IPR008979","properties":[{"key":"EntryName","value":"Galactose-bd-like_sf"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR001547","properties":[{"key":"EntryName","value":"Glyco_hydro_5"}]},{"database":"InterPro","id":"IPR013783","properties":[{"key":"EntryName","value":"Ig-like_fold"}]},{"database":"InterPro","id":"IPR001119","properties":[{"key":"EntryName","value":"SLH_dom"}]},{"database":"PANTHER","id":"PTHR43308","properties":[{"key":"EntryName","value":"OUTER MEMBRANE PROTEIN ALPHA-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43308:SF5","properties":[{"key":"EntryName","value":"S-LAYER PROTEIN _ PEPTIDOGLYCAN ENDO-BETA-N-ACETYLGLUCOSAMINIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02018","properties":[{"key":"EntryName","value":"CBM_4_9"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00150","properties":[{"key":"EntryName","value":"Cellulase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00395","properties":[{"key":"EntryName","value":"SLH"},{"key":"MatchStatus","value":"3"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49785","properties":[{"key":"EntryName","value":"Galactose-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51272","properties":[{"key":"EntryName","value":"SLH"},{"key":"MatchStatus","value":"3"}]}],"sequence":{"value":"MKKVLSKLMVFVMVLTVALGNGVFIGDKQAKAAGTSGDGRFHVVGNKIVDPDGNDFVIKGVNIQGYRSWEKRSVLQDVHLIADVWKFNTVRLNCFIGQNNWGEGTGANNDIDAIIKAFTAKKVVVEIDLHDTTGYPPLSNPPPAPGQPSLDQAIAWFKELAAKYKDNPYVWFNTMNEPGSSTAPLDPQWKVANEEIIKAIRSTGADNIIVVDGWSYANEGIEQNTPTVDEKRSAVLTYGQDLLNADSAKNTIFAFHNYNEGDIQKKVEDYIDRANAKGLYVFMEEYGKDYSDAAKEGVKSGLQAVMNKGAGRIYWNWDGYDLYDLTSGTGRGSGWEINKTDGSKPTNLSWVGDKIWDDNHGITPTFDDQNPKVDLALERLIANNNGFKAGDKVQFTTFLRNSGDLPIGKDSKVVVKFYVDGVQLGDPVEISGGIAVGQRIPVTSPELTVSKTDFTVKAVIDSSSTYADGAEDAVIENNWIEAAFNSTAPSSGYELVVTGIKITPDTVKERDYVQAQVTVANQGPEATPVTNIIGWFYVNGYYYTLDDAAKSCAEQDNVTLKPGESITLSTKVKYRAAAPCNFSFVLENLYADDQNQSNNSITVNVPVKMGEGGVNMVSNPGFEDGLDSWQDWQQDMSAVPEAAHNGALGLKIGGGKAAGGGQDIPLKPNTTYILGAWAKFDSKPAGTFDVVVQYHLKDANNTYVQHILNFNETDWTYKQLLFTTPDVFGSTPQLALWKGDTSKANLYVDDVYLVEVSNLIVNGTAENGMDGWPDWGYPVSAVPEAAYGGTKGFKLSGGKQAGMGQKVALKPNTTYILGAWGKFTAKPGTYCDVIVQYHLKDANNTYVQNILRFTETDWTYKQVVFTTPDAFGSDPEFVLWKDDASNADFYADNITLVEVPSSMVNKGSIAPKFTDISSSWAKNEIQVLASKNIISGYPDGTFKPDKRITRAEFVSMLVKALGIKQSIPDVPTFSDVNKGDWYYGLVEAAKSTGIASGYGKQFKPDMQITRQEMMVMVVNALRVNKVEKFVSKGDVSVLGKFKDGGKVQNWAKDAMAIGVSNGLIKGTGDEYLSPDGRATRAQAAAVIYRMLLQLGRI","length":1097,"molWeight":119763,"crc64":"C41C6EB92C0494B9","md5":"A525778B1FD1E6C95654597F926D9B97"},"extraAttributes":{"countByFeatureType":{"Signal":1,"Chain":1,"Domain":3,"Binding site":10},"uniParcId":"UPI00000AEFB9"}}]}