{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O69262","uniProtkbId":"TXABF_THEXY","entryAudit":{"firstPublicDate":"2026-11-04","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2001-03-01","entryVersion":86,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Thermobacillus xylanilyticus","taxonId":76633,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Thermobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10742272"}],"value":"Alpha-L-arabinofuranosidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10742272"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11842234"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18563919"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23628811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140392"}],"value":"3.2.1.55"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10742272"}],"value":"AbfD3"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18563919"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"22823427"}],"value":"TxAbf"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18563919"}],"value":"AbjA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10742272"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11842234"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18563919"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23628811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140392"}],"value":"Glycosidase that catalyzes the hydrolysis of alpha-L-arabinofuranosyl side chains in xylans (PubMed:10742272). Is extremely active on wheat arabinoxylan, larchwood xylan and oat spelt xylan (PubMed:10742272). In vitro, it catalyzes the hydrolysis of the synthetic compound p-nitrophenyl-alpha-L-arabinofuranoside (pNP-alpha-L-Ara) (PubMed:10742272, PubMed:11842234, PubMed:18563919, PubMed:22823427, PubMed:23628811, PubMed:24140392). Shows weak activity with p-nitrophenyl-beta-D-galactofuranoside as substrate (PubMed:22823427). It cannot hydrolyze p-nitrophenyl-alpha-L-arabinopyranoside or gum arabic (PubMed:10742272). The enzyme exhibits low transglycosylation activity, but the product is subject to secondary hydrolysis (PubMed:23628811)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.","ecNumber":"3.2.1.55","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10742272"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11842234"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18563919"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23628811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140392"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10742272"}],"value":"Activity is not affected by EDTA or divalent cations, such as Ca(2+), Mg(2+), Zn(2+) and Ni(2+), suggesting that the enzyme does not require metal cofactors (PubMed:10742272). Activity is partially inhibited by Cu(2+) and Co(2+), and strongly inhibited by HgCl(2) (PubMed:10742272). Activity is unaffected by dithiothreitol or beta-mercaptoethanol (PubMed:10742272)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":456.0,"unit":"umol/min/mg","enzyme":"enzyme with p-nitrophenyl-alpha-L-arabinofuranoside as substrate (at 60 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10742272"}]},{"velocity":555.0,"unit":"umol/min/mg","enzyme":"enzyme with p-nitrophenyl-alpha-L-arabinofuranoside as substrate (at 75 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10742272"}]}],"michaelisConstants":[{"constant":0.72,"unit":"mM","substrate":"p-nitrophenyl-alpha-L-arabinofuranoside (at 60 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10742272"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"}]},{"constant":0.5,"unit":"mM","substrate":"p-nitrophenyl-alpha-L-arabinofuranoside (at 75 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10742272"}]},{"constant":0.7,"unit":"mM","substrate":"p-nitrophenyl-alpha-L-arabinofuranoside","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11842234"}]},{"constant":1.4,"unit":"mM","substrate":"p-nitrophenyl-alpha-L-arabinofuranoside","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18563919"}]},{"constant":0.27,"unit":"mM","substrate":"p-nitrophenyl-alpha-L-arabinofuranoside","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140392"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11842234"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18563919"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140392"}],"value":"kcat is 4100 sec(-1) with p-nitrophenyl-alpha-L-arabinofuranoside as substrate (PubMed:11842234). kcat is 355 sec(-1) with p-nitrophenyl-alpha-L-arabinofuranoside as substrate (PubMed:18563919). kcat is 575 sec(-1) with p-nitrophenyl-alpha-L-arabinofuranoside as substrate (PubMed:22823427). kcat is 431 sec(-1) with p-nitrophenyl-alpha-L-arabinofuranoside as substrate (PubMed:24140392)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10742272"}],"value":"Optimum pH is 5.6 to 6.2 (PubMed:10742272). Is stable in the pH range 4 to 11 (PubMed:10742272)."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10742272"}],"value":"Optimum temperature is 75 degrees Celsius (PubMed:10742272). Is highly stable up to 90 degrees Celsius (PubMed:10742272)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10742272"}],"value":"Glycan degradation; xylan degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18563919"}],"value":"Homohexamer; dimer of trimers"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18563919"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"}],"value":"Contains a catalytic domain that is folded into a (beta/alpha)8-barrel and a C-terminal domain that displays jelly roll architecture (PubMed:18563919). In the absence of substrate, the enzyme adopts an open conformation (PubMed:18563919). In the substrate-bound form, the long loop connecting beta-strand 2 to alpha-helix 2 closes the active site and interacts with the substrate through residues His-98 and Trp-99 (PubMed:18563919). Residues His-98 and Trp-99 are key determinants of catalysis: His-98 contributes to dynamic active-site organization, whereas Trp-99 is involved in substrate binding and in the formation of a functional active site (PubMed:22823427)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18563919"}],"value":"Contains a disulfide bridge (Cys-74-Cys-180) in the active site; it may ensure correct orientation of the catalytic acid/base residue Glu-176"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23628811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140392"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33524585"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34482168"}],"value":"Could be used as a synthetic tool for glycochemistry (PubMed:23628811, PubMed:24140392, PubMed:33524585, PubMed:34482168). Mutants have been developed to shift the catalytic activity from hydrolysis toward transglycosylation, a reaction useful for the synthesis of complex carbohydrates (PubMed:23628811, PubMed:24140392, PubMed:33524585, PubMed:34482168). The objective is to reduce competing hydrolytic activity while maintaining or enhancing glycosyl transfer activity, thereby favoring product accumulation (PubMed:23628811, PubMed:24140392, PubMed:33524585, PubMed:34482168). Mutants bearing N216W synthesize not only (1,2)-linked furanobiosides, but also (1,3)- and even (1,5)-linked furanobiosides (PubMed:34482168)"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 51 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":496,"modifier":"EXACT"}},"description":"Alpha-L-arabinofuranosidase","featureId":"PRO_0000464964"},{"type":"Active site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11842234"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"18563919"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"33524585"}]},{"type":"Active site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11842234"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"33524585"}]},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:28772"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33524585"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6ZT7"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6ZT9"}],"ligand":{"name":"alpha-L-arabinofuranose","id":"ChEBI:CHEBI:28772"}},{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:28772"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33524585"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6ZT7"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6ZT9"}],"ligand":{"name":"alpha-L-arabinofuranose","id":"ChEBI:CHEBI:28772"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:28772"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33524585"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6ZT7"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6ZT9"}],"ligand":{"name":"alpha-L-arabinofuranose","id":"ChEBI:CHEBI:28772"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:28772"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33524585"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6ZT7"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6ZT9"}],"ligand":{"name":"alpha-L-arabinofuranose","id":"ChEBI:CHEBI:28772"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:28772"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33524585"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6ZT7"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6ZT9"}],"ligand":{"name":"alpha-L-arabinofuranose","id":"ChEBI:CHEBI:28772"}},{"type":"Site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"Important for activity","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11842234"}]},{"type":"Site","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Important for activity","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"18563919"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22823427"}]},{"type":"Site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"Important for activity","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"18563919"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22823427"}]},{"type":"Disulfide bond","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18563919"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2VRK"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2VRQ"}]},{"type":"Mutagenesis","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"9700-fold decrease in catalytic efficiency with pNP-alpha-L-Ara as substate. Loss of activity; when associated with A-176.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11842234"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"2800-fold decrease in catalytic efficiency with pNP-alpha-L-Ara as substate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11842234"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["D"]}},{"type":"Mutagenesis","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"Almost loss of activity with pNP-alpha-L-Ara as substrate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11842234"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"No change in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11842234"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"81-fold decrease in catalytic efficiency with pNP-alpha-L-Ara as substate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"}],"alternativeSequence":{"originalSequence":"HW","alternativeSequences":["AA"]}},{"type":"Mutagenesis","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"28-fold decrease in catalytic efficiency with pNP-alpha-L-Ara as substate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"}],"alternativeSequence":{"originalSequence":"HW","alternativeSequences":["FF"]}},{"type":"Mutagenesis","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"6-fold decrease in catalytic efficiency with pNP-alpha-L-Ara as substate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"3.5-fold decrease in catalytic efficiency with pNP-alpha-L-Ara as substate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["F"]}},{"type":"Mutagenesis","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"70-fold decrease in catalytic efficiency with pNP-alpha-L-Ara as substate. 53-fold decrease in catalytic efficiency with pNP-alpha-L-Ara as substate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18563919"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"}],"alternativeSequence":{"originalSequence":"W","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"44-fold decrease in catalytic efficiency with pNP-alpha-L-Ara as substate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22823427"}],"alternativeSequence":{"originalSequence":"W","alternativeSequences":["F"]}},{"type":"Mutagenesis","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"No change in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11842234"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"No change in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11842234"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"6600-fold decrease in catalytic efficiency with pNP-alpha-L-Ara as substate. 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Displays a severely reduced ability to perform secondary hydrolysis, which leads to higher transglycosylation yields. Shows altered pH optimum.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140392"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["P"]}},{"type":"Mutagenesis","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"60-fold decrease in catalytic efficiency with pNP-alpha-L-Ara as substate. Displays a severely reduced ability to perform secondary hydrolysis, which leads to higher transglycosylation yields. Shows altered pH optimum.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24140392"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["Y"]}}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0624","category":"Biological process","name":"Polysaccharide degradation"},{"id":"KW-0858","category":"Biological process","name":"Xylan degradation"}],"references":[{"referenceNumber":1,"citation":{"id":"10446364","citationType":"journal article","authors":["Connerton I.F.","Cummings N.J.","Harris G.W.","Debeire P.","Breton C."],"citationCrossReferences":[{"database":"PubMed","id":"10446364"},{"database":"DOI","id":"10.1016/s0167-4838(99)00151-x"}],"title":"A single domain thermophilic xylanase can bind insoluble xylan: evidence for surface aromatic clusters.","publicationDate":"1999","journal":"Biochim. 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The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Binds 4 Mg(2+) or Mn(2+) ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. 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The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"CAG5079007.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary 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