{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O08342","uniProtkbId":"GUNA_PAEBA","entryAudit":{"firstPublicDate":"2009-05-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1997-07-01","entryVersion":82,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Endoglucanase A"},"ecNumbers":[{"value":"3.2.1.4"}]},"alternativeNames":[{"fullName":{"value":"Cellulase A"}},{"fullName":{"value":"Endo-1,4-beta-D-glucanase A"}}],"flag":"Precursor"},"genes":[{"geneName":{"value":"celA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9720200"}],"value":"Endoglucanase with high activity on carboxymethylcellulose (CMC) and lichenan, but not active on Avicel"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.","ecNumber":"3.2.1.4","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9720200"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9720200"}],"value":"Strongly inhibited by Hg(2+), Ag(+) and Fe(3+). To a lesser extent, is also inhibited by Pb(2+), Mn(2+), Sn(2+) and Cu(2+). By contrast, Ni(2+), Zn(2+), Co(2+), Ba(2+) and NH(4)(+) do not affect enzyme activity, while 10 mM Ca(2+), and Mg(2+) produce a stimulating effect. Is also strongly inhibited by chemicals such as N-bromosuccinimide and dimethyl(2-dihydroxy-5-nitrobenzyl)sulphonium bromide. Is not affected by N-acetylimidazole"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9720200"}],"value":"Optimum pH is 4.0. Highly stable at acid pH. Retains 100% of its activity after 90 minutes incubation at pH 4.5 and 45 degrees Celsius, and 95% of the initial activity is found after 15 days incubation at room temperature and pH 4.5."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9720200"}],"value":"Optimum temperature is 40 degrees Celsius. Shows 98% and 51% of its maximum activity at 45 and 55 degrees Celsius, respectively."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9720200"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9720200"}],"value":"Study of the performance of endoglucanase A on paper manufacture from agricultural fibers shows that treatment with the enzyme improves the properties of the pulp and the quality of paper. CelA treatment enhances the physical properties (stretch and tensile index) of paper from wheat straw, while dewatering properties are slightly diminished"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 5 (cellulase A) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Chain","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":400,"modifier":"EXACT"}},"description":"Endoglucanase A","featureId":"PRO_0000371421"},{"type":"Active site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}],"keywords":[{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"id":"KW-0136","category":"Biological process","name":"Cellulose degradation"},{"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-0964","category":"Cellular component","name":"Secreted"},{"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"9720200","citationType":"journal article","authors":["Blanco A.","Diaz P.","Martinez J.","Vidal T.","Torres A.L.","Pastor F.I.J."],"citationCrossReferences":[{"database":"PubMed","id":"9720200"},{"database":"DOI","id":"10.1007/s002530051255"}],"title":"Cloning of a new endoglucanase gene from Bacillus sp. BP-23 and characterisation of the enzyme. Performance in paper manufacture from cereal straw.","publicationDate":"1998","journal":"Appl. Microbiol. Biotechnol.","firstPage":"48","lastPage":"54","volume":"50"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","BIOTECHNOLOGY","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","SUBCELLULAR LOCATION"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"Y12512","properties":[{"key":"ProteinId","value":"CAA73113.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110895944.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"O08342","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O08342","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH5","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 5"}]},{"database":"OrthoDB","id":"9800955at2","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:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008422","properties":[{"key":"GoTerm","value":"F:beta-glucosidase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008810","properties":[{"key":"GoTerm","value":"F:cellulase 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":"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":"IPR018087","properties":[{"key":"EntryName","value":"Glyco_hydro_5_CS"}]},{"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"}]},{"database":"PROSITE","id":"PS00659","properties":[{"key":"EntryName","value":"GLYCOSYL_HYDROL_F5"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKTFKKFSIAGLALLFMATAAFAGWSTKASAADMRSLTAAQITAEMGAGWNLGNQLEATVNGTPNETSWGNPTITPELIKKVKAAGFKTIRIPVSYLNYIGSAPNYTVNASWLNRIQQVVDYAYNEGLYVVINMHGDGFHSIPGSWLHVNSSNQNVIRDKYQKVWQQVATRFSAYNERLIFESMNEVFDGNYNNPNTSYYGNLNAYNQIFVDTVRKTGGNNNARWLLVPGWNTNIDYTVGNYGFVVPTDNFRSSAIPSSQKRIMISAHYYSPWDFAGEENGNITQWGATATNPAKRSTWGQEDYLDSQFKSMYDKFVTQGYPVVMGEFGSIDKSSYDSSNNNYRAVYAKAVTATAKKYKLVPVYWDNGFNGQHGFALFNRFNNTVTQQNIINAIMQGMQ","length":400,"molWeight":44799,"crc64":"E89CB35BBC6F8AE5","md5":"7AE481E84102FEFF5CF1EA3DA0AF71FD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBCELLULAR LOCATION":1,"BIOTECHNOLOGY":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Active site":2},"uniParcId":"UPI00000B3457"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9X6Z2","uniProtkbId":"PLYA_PAEBA","entryAudit":{"firstPublicDate":"2009-03-24","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1999-11-01","entryVersion":71,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Pectate lyase A"},"ecNumbers":[{"value":"4.2.2.2"}]},"alternativeNames":[{"fullName":{"value":"Pectin lyase"},"ecNumbers":[{"value":"4.2.2.10"}]}],"flag":"Precursor"},"genes":[{"geneName":{"value":"pelA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10658655"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16514142"}],"value":"Catalyzes the depolymerization of both polygalacturonate and pectins of methyl esterification degree from 22 to 89%, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins. Is not able to cleave trigalacturonate. Does not degrade xylans and carboxymethylcellulose (CMC)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.","ecNumber":"4.2.2.2"}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.","ecNumber":"4.2.2.10"}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10658655"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16514142"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10658655"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16514142"}],"value":"Binds 1 Ca(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10658655"}],"value":"Strongly inhibited by Ba(2+). To a lesser extent, is also inhibited by Sn(2+), Mg(2+) and Ag(+). Inhibited by EDTA in vitro"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":102.4,"unit":"umol/min/mg","enzyme":"enzyme with 22% esterified pectin as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10658655"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16514142"}]},{"velocity":95.4,"unit":"umol/min/mg","enzyme":"enzyme with polygalacturonic acid as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10658655"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16514142"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10658655"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16514142"}],"value":"Optimum pH is 10. Is stable for 1 hour at 40 degrees Celsius in the pH range 4.0-8.0."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10658655"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16514142"}],"value":"Optimum temperature is 50-55 degrees Celsius. More than 50% of maximum activity is found in the temperature range 40-60 degrees Celsius. Retains more than 50% of the initial activity after 4 hours incubation at 40 degrees Celsius at pH 10, while at 50 degrees Celsius only 1% of the initial activity is found after the same treatment."}]}},{"texts":[{"value":"Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the polysaccharide lyase 3 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"Pectate lyase A","featureId":"PRO_5000065163"}],"keywords":[{"id":"KW-0106","category":"Ligand","name":"Calcium"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"10658655","citationType":"journal article","authors":["Soriano M.","Blanco A.","Diaz P.","Pastor F.I.J."],"citationCrossReferences":[{"database":"PubMed","id":"10658655"},{"database":"DOI","id":"10.1099/00221287-146-1-89"}],"title":"An unusual pectate lyase from a Bacillus sp. with high activity on pectin: cloning and characterization.","publicationDate":"2000","journal":"Microbiology","firstPage":"89","lastPage":"95","volume":"146"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","SUBSTRATE SPECIFICITY","COFACTOR","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"16514142","citationType":"journal article","authors":["Soriano M.","Diaz P.","Pastor F.I.J."],"citationCrossReferences":[{"database":"PubMed","id":"16514142"},{"database":"DOI","id":"10.1099/mic.0.28562-0"}],"title":"Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin.","publicationDate":"2006","journal":"Microbiology","firstPage":"617","lastPage":"625","volume":"152"},"referencePositions":["FUNCTION","SUBSTRATE SPECIFICITY","COFACTOR","BIOPHYSICOCHEMICAL PROPERTIES"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ237980","properties":[{"key":"ProteinId","value":"CAB40884.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_174812328.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"Q9X6Z2","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9X6Z2","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"PL3","properties":[{"key":"FamilyName","value":"Polysaccharide Lyase Family 3"}]},{"database":"BRENDA","id":"4.2.2.2","properties":[{"key":"OrganismId","value":"22107"}]},{"database":"UniPathway","id":"UPA00545","properties":[{"key":"RectionId","value":"UER00824"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0030570","properties":[{"key":"GoTerm","value":"F:pectate lyase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0047490","properties":[{"key":"GoTerm","value":"F:pectin lyase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0045490","properties":[{"key":"GoTerm","value":"P:pectin catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"FunFam","id":"2.160.20.10:FF:000044","properties":[{"key":"EntryName","value":"Pectate lyase E"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.20.10","properties":[{"key":"EntryName","value":"Single-stranded right-handed beta-helix, Pectin lyase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004898","properties":[{"key":"EntryName","value":"Pectate_lyase_PlyH/PlyE-like"}]},{"database":"InterPro","id":"IPR012334","properties":[{"key":"EntryName","value":"Pectin_lyas_fold"}]},{"database":"InterPro","id":"IPR011050","properties":[{"key":"EntryName","value":"Pectin_lyase_fold/virulence"}]},{"database":"PANTHER","id":"PTHR33407","properties":[{"key":"EntryName","value":"PECTATE LYASE F-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33407:SF9","properties":[{"key":"EntryName","value":"PECTATE LYASE F-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03211","properties":[{"key":"EntryName","value":"Pectate_lyase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51126","properties":[{"key":"EntryName","value":"Pectin lyase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKMLTLLLSAGLVASIFGVMPAAAAPTVVNSTIVVPKGTTYDGQGKTFVANPSTLGDGSQAENQKPVFRLEAGATLKNVIIGAPAADGVHCYGSCNISNVVWEDVGEDALTLKSSGTVNITGGAAYKAYDKVFQMNASGTINIKNFRADDIGKLVRQNGGTSYAVNMTLDNSNISNVKDSIMRTDSSVSQGKITNTRYSKVPTLFKGFASGKTSQSGNTQY","length":222,"molWeight":23233,"crc64":"7F29F585791C9682","md5":"3BF3F095D47634A6BC73C6996E30845D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1},"uniParcId":"UPI00000B2D11"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"V9TXH2","uniProtkbId":"XYN11_PAEBA","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2014-03-19","entryVersion":44,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24549767"}],"value":"Endo-1,4-beta-xylanase Xyn11E"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24549767"}],"value":"3.2.1.8"}]},"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24549767"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AHC74025.1"}],"value":"xyn11E"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"PYE48003.1"}],"value":"DFQ00_11065"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24549767"}],"value":"Involved in depolymerization of xylan, a major component of the lignocellulosic substrates. Acts as an endo-xylanase that efficiently hydrolyzes the beta-1,4 glycosidic linkages between the xylopyranosyl residues in the main chain of the polymer, leading to the degradation of xylan into short oligosaccharides. Shows high activity toward branched xylans from both softwoods (arabinoxylans) and hardwoods (glucuronoxylans), showing the highest activity on beechwood xylan. Also hydrolyzes long xylooligosaccharides (with a degree of polymerization of greater than or equal to 5), while oligomers shorter than xylotetraose are not degraded. Is not active on carboxymethyl cellulose (CMC), Avicel, starch, polygalacturonic acid, laminarin, pectin, beta-D-barley glucan, or lichenan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.","ecNumber":"3.2.1.8","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24549767"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":3023.0,"unit":"umol/min/mg","enzyme":"enzyme for the hydrolysis of beechwood xylan","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24549767"}]}],"michaelisConstants":[{"constant":12.98,"unit":"mg/ml","substrate":"beechwood xylan","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24549767"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24549767"}],"value":"Optimum pH is 6.5."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24549767"}],"value":"Optimum temperature is 50 degrees Celsius. Retains about 80% of the activity after incubation for 2 hours at 50 degrees Celsius, but is rapidly inactivated at higher temperatures."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24549767"}],"value":"Glycan degradation; xylan degradation"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24549767"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24549767"}],"value":"This enzyme liberates reducing sugars from elemental chlorine free (ECF) and totally chlorine free (TCF) bleached pulps from eucalyptus, sisal, and flax, which makes it a good candidate for the enzymatic-assisted production of high-cellulose-content pulps from paper-grade pulps"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24549767"}],"value":"Is dependent on P.barcinonensis lipoprotein LppX for its expression in an active form"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 11 (cellulase G) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"Endo-1,4-beta-xylanase Xyn11E","featureId":"PRO_5016557792"},{"type":"Domain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"GH11","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01097"}]},{"type":"Active site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01097"},{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10062"}]},{"type":"Active site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01097"},{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10062"}]}],"keywords":[{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"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-0964","category":"Cellular component","name":"Secreted"},{"id":"KW-0732","category":"Domain","name":"Signal"},{"id":"KW-0858","category":"Biological process","name":"Xylan degradation"}],"references":[{"referenceNumber":1,"citation":{"id":"24549767","citationType":"journal article","authors":["Valenzuela S.V.","Diaz P.","Pastor F.I."],"citationCrossReferences":[{"database":"PubMed","id":"24549767"},{"database":"DOI","id":"10.1007/s00253-014-5565-2"}],"title":"Xyn11E from Paenibacillus barcinonensis BP-23: a LppX-chaperone-dependent xylanase with potential for upgrading paper pulps.","publicationDate":"2014","journal":"Appl. Microbiol. Biotechnol.","firstPage":"5949","lastPage":"5957","volume":"98"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","BIOPHYSICOCHEMICAL PROPERTIES","PATHWAY","BIOTECHNOLOGY"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"26203337","citationType":"journal article","authors":["Whitman W.B.","Woyke T.","Klenk H.P.","Zhou Y.","Lilburn T.G.","Beck B.J.","De Vos P.","Vandamme P.","Eisen J.A.","Garrity G.","Hugenholtz P.","Kyrpides N.C."],"citationCrossReferences":[{"database":"PubMed","id":"26203337"},{"database":"DOI","id":"10.1186/s40793-015-0017-x"}],"title":"Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III: the genomes of soil and plant-associated and newly described type strains.","publicationDate":"2015","journal":"Stand. Genomic Sci.","firstPage":"26","lastPage":"26","volume":"10"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KF766535","properties":[{"key":"ProteinId","value":"AHC74025.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"QJSW01000010","properties":[{"key":"ProteinId","value":"PYE48003.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110897546.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"V9TXH2","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"V9TXH2","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH11","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 11"}]},{"database":"OrthoDB","id":"9806342at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00114","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0031176","properties":[{"key":"GoTerm","value":"F:endo-1,4-beta-xylanase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"24549767"}]},{"database":"GO","id":"GO:0045493","properties":[{"key":"GoTerm","value":"P:xylan catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"24549767"}]},{"database":"FunFam","id":"2.60.120.180:FF:000001","properties":[{"key":"EntryName","value":"Endo-1,4-beta-xylanase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.180","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013320","properties":[{"key":"EntryName","value":"ConA-like_dom_sf"}]},{"database":"InterPro","id":"IPR013319","properties":[{"key":"EntryName","value":"GH11/12"}]},{"database":"InterPro","id":"IPR018208","properties":[{"key":"EntryName","value":"GH11_AS_1"}]},{"database":"InterPro","id":"IPR033119","properties":[{"key":"EntryName","value":"GH11_AS_2"}]},{"database":"InterPro","id":"IPR033123","properties":[{"key":"EntryName","value":"GH11_dom"}]},{"database":"InterPro","id":"IPR001137","properties":[{"key":"EntryName","value":"Glyco_hydro_11"}]},{"database":"PANTHER","id":"PTHR46828","properties":[{"key":"EntryName","value":"ENDO-1,4-BETA-XYLANASE A-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46828:SF2","properties":[{"key":"EntryName","value":"ENDO-1,4-BETA-XYLANASE A-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00457","properties":[{"key":"EntryName","value":"Glyco_hydro_11"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00911","properties":[{"key":"EntryName","value":"GLHYDRLASE11"}]},{"database":"SUPFAM","id":"SSF49899","properties":[{"key":"EntryName","value":"Concanavalin A-like lectins/glucanases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00776","properties":[{"key":"EntryName","value":"GH11_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00777","properties":[{"key":"EntryName","value":"GH11_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51761","properties":[{"key":"EntryName","value":"GH11_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFKFGKKLMTVVLAASMSFGVFAATTGATDYWQNWTDGGGTVNAVNGSGGNYSVNWQNTGNFVVGKGWTYGTPNRVVNYNAGVFSPSGNGYLTFYGWTRNALIEYYVVDNWGTYRPTGTYKGTVNSDGGTYDIYTTMRYNQPSIDGYSTFPQYWSVRQSKRPIGVNSQITFQNHVNAWASKGMNLGSSWSYQVLATEGYQSSGSSNVTVW","length":210,"molWeight":23145,"crc64":"E3454EC152DFEB41","md5":"87A2B2E16A288371DC0DBCFE66466B0A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"BIOTECHNOLOGY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1,"Active site":2},"uniParcId":"UPI0003D7F8CB"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O69231","uniProtkbId":"XYNB_PAEBA","entryAudit":{"firstPublicDate":"2009-03-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-08-01","entryVersion":85,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Endo-1,4-beta-xylanase B"},"shortNames":[{"value":"Xylanase B"}],"ecNumbers":[{"value":"3.2.1.8"}]},"alternativeNames":[{"fullName":{"value":"1,4-beta-D-xylan xylanohydrolase B"}}]},"genes":[{"geneName":{"value":"xynB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12698280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8998999"}],"value":"Plays a role in plant xylan biodegradation, probably via the hydrolysis of short xylooligosaccharides resulting from extracellular xylan hydrolysis, once they have been transported inside cells. Shows similar activity on xylans of different rate of arabinose or methylglucuronic substitution. Also displays high activity on aryl-xylosides. Is active on xylotetraose and xylotriose, but does not hydrolyze xylobiose, indicating that XynB is a xylanase and not a beta-xylosidase"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.","ecNumber":"3.2.1.8","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12698280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8998999"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8998999"}],"value":"Completely inhibited by Ag(2+), Cu(2+), Hg(2+), Mn(2+), Pb(2+) and Sn(2+). Strongly inhibited by Fe(2+) and Zn(2+). Co(2+) and Ni(2+) cause little inhibition while Ca(2+) and Mg(2+) do not affect enzyme activity, and Ba(2+) produces a small stimulating effect. Irreversibly inactivated by SDS in vitro"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8998999"}],"value":"Optimum pH is 5.5. Shows more than 75% of maximum activity from pH 5 to 10. Is still active at pH 12."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8998999"}],"value":"Optimum temperature is 50 degrees Celsius. Loses 100% activity after incubation for 15 minutes at 50 degrees Celsius."}]}},{"texts":[{"value":"Glycan degradation; xylan degradation"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"value":"Is not secreted to the medium but instead remains cell-associated, in the soluble fraction, even in late stationary-phase cultures"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12698280"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 10 (cellulase F) family. Cytoplasmic xylanase subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12698280"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"Endo-1,4-beta-xylanase B","featureId":"PRO_0000366196"},{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"GH10","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01096"}]},{"type":"Active site","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Helix","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Turn","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Helix","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Helix","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMQ"}]},{"type":"Helix","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Turn","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Helix","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Helix","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Turn","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Helix","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Helix","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Helix","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Helix","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Turn","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMC"}]},{"type":"Beta strand","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Helix","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Turn","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Helix","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Beta strand","location":{"start":{"value":313,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]},{"type":"Helix","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3EMZ"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"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":"12698280","citationType":"journal article","authors":["Gallardo O.","Diaz P.","Pastor F.I.J."],"citationCrossReferences":[{"database":"PubMed","id":"12698280"},{"database":"DOI","id":"10.1007/s00253-003-1239-1"}],"title":"Characterization of a Paenibacillus cell-associated xylanase with high activity on aryl-xylosides: a new subclass of family 10 xylanases.","publicationDate":"2003","journal":"Appl. Microbiol. Biotechnol.","firstPage":"226","lastPage":"233","volume":"61"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-11","FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","SUBCELLULAR LOCATION"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"8998999","citationType":"journal article","authors":["Blanco A.","Diaz P.","Martinez J.","Lopez O.","Soler C.","Pastor F.I.J."],"citationCrossReferences":[{"database":"PubMed","id":"8998999"},{"database":"DOI","id":"10.1111/j.1574-6968.1996.tb08120.x"}],"title":"Cloning of a Bacillus sp. BP-23 gene encoding a xylanase with high activity against aryl xylosides.","publicationDate":"1996","journal":"FEMS Microbiol. Lett.","firstPage":"285","lastPage":"290","volume":"137"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ006646","properties":[{"key":"ProteinId","value":"CAA07174.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110896347.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"PDB","id":"3EMC","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.10 A"},{"key":"Chains","value":"A=2-332"}]},{"database":"PDB","id":"3EMQ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.73 A"},{"key":"Chains","value":"A=2-332"}]},{"database":"PDB","id":"3EMZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.08 A"},{"key":"Chains","value":"A=2-332"}]},{"database":"AlphaFoldDB","id":"O69231","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O69231","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH10","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 10"}]},{"database":"OrthoDB","id":"9809277at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00114","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"O69231","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:0031176","properties":[{"key":"GoTerm","value":"F:endo-1,4-beta-xylanase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0045493","properties":[{"key":"GoTerm","value":"P:xylan catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR044846","properties":[{"key":"EntryName","value":"GH10"}]},{"database":"InterPro","id":"IPR001000","properties":[{"key":"EntryName","value":"GH10_dom"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"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":"PF00331","properties":[{"key":"EntryName","value":"Glyco_hydro_10"},{"key":"MatchStatus","value":"1"}]},{"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":"PROSITE","id":"PS51760","properties":[{"key":"EntryName","value":"GH10_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTEIPSLSASYANSFKIGAAVHTRMLQTEGEFIAKHYNSVTAENQMKFEEVHPREHEYTFEAADEIVDFAVARGIGVRGHTLVWHNQTPAWMFEDASGGTASREMMLSRLKQHIDTVVGRYKDQIYAWDVVNEAIEDKTDLIMRDTKWLRLLGEDYLVQAFNMAHEADPNALLFYNDYNETDPVKREKIYNLVRSLLDQGAPVHGIGMQGHWNIHGPSMDEIRQAIERYASLDVQLHVTELDLSVFRHEDQRTDLTEPTAEMAELQQKRYEDIFGLFREYRSNITSVTFWGVADNYTWLDNFPVRGRKNWPFVFDTELQPKDSFWRIIGQD","length":332,"molWeight":38561,"crc64":"DDEF7BCF17C8A72E","md5":"D12F3F78B2E5D2C824DA3FA19A74269B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Domain":1,"Active site":2,"Helix":13,"Turn":5,"Beta strand":14},"uniParcId":"UPI00000B3BCC"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O69230","uniProtkbId":"XYNC_PAEBA","entryAudit":{"firstPublicDate":"2009-05-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-08-01","entryVersion":108,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Endo-1,4-beta-xylanase C"},"shortNames":[{"value":"Xylanase C"}],"ecNumbers":[{"value":"3.2.1.8"}]},"alternativeNames":[{"fullName":{"value":"1,4-beta-D-xylan xylanohydrolase C"}}],"flag":"Precursor"},"genes":[{"geneName":{"value":"xynC"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10463183"}],"value":"Endoxylanase with high hydrolytic activity on birchwood and oat spelt xylan. Xylotetraose, xylotriose, xylobiose and xylose are the main products from birchwood xylan hydrolysis. Shows increasing activity on xylo-oligosaccharides of increasing length. Displays very low hydrolytic activity on Avicel, carboxymethylcellulose (CMC) and p-nitrophenyl-beta-xylopyranoside. Also shows transxylosidase activity, allowing the formation of xylo-oligosaccharides of higher degree of polymerization than the starting substrate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.","ecNumber":"3.2.1.8","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10463183"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10463183"}],"value":"Optimum pH is 5. Retains at least 50% of its maximum activity between pH 4.5 and 8.0. Is not active at pH values below 4.5, while at least 35% of maximum activity is found in the pH range 8.5-11.0."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10463183"}],"value":"Optimum temperature is 45 degrees Celsius. Is only stable at 55 degrees Celsius or lower temperatures. Retains more than 77% activity after 2 hours incubation at 55 degrees Celsius and pH 7."}]}},{"texts":[{"value":"Glycan degradation; xylan degradation"}],"commentType":"PATHWAY"},{"texts":[{"value":"Consists of three different domains. The central region of the enzyme is the catalytic domain. The N-terminal region contains cenC-type cellulose-binding domains and seems to act as a thermostabilizing domain: a derivative lacking this region shows a lower optimum temperature for activity (35 degrees Celsius) than the full-length enzyme, and a reduced thermal stability that results in a complete inactivation of the enzyme after 2 hours incubation at 55 degrees Celsius. The C-terminal region contains family 9 carbohydrate-binding modules"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 10 (cellulase F) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":1086,"modifier":"EXACT"}},"description":"Endo-1,4-beta-xylanase C","featureId":"PRO_0000371420"},{"type":"Domain","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"CBM-cenC 1"},{"type":"Domain","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"CBM-cenC 2"},{"type":"Domain","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":710,"modifier":"EXACT"}},"description":"GH10","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01096"}]},{"type":"Active site","location":{"start":{"value":502,"modifier":"EXACT"},"end":{"value":502,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":556,"modifier":"EXACT"},"end":{"value":556,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":620,"modifier":"EXACT"},"end":{"value":620,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10061"}]},{"type":"Beta strand","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Turn","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUO"}]},{"type":"Beta strand","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Beta strand","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Beta strand","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Beta strand","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Beta strand","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Helix","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Beta strand","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Beta strand","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Beta strand","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Beta strand","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Helix","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Beta strand","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Helix","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":340,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Helix","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Beta strand","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4XUR"}]},{"type":"Helix","location":{"start":{"value":371,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":387,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":395,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":415,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":443,"modifier":"EXACT"},"end":{"value":447,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":452,"modifier":"EXACT"},"end":{"value":454,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":457,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":472,"modifier":"EXACT"},"end":{"value":490,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Turn","location":{"start":{"value":491,"modifier":"EXACT"},"end":{"value":493,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":496,"modifier":"EXACT"},"end":{"value":501,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":508,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":515,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":519,"modifier":"EXACT"},"end":{"value":523,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":534,"modifier":"EXACT"},"end":{"value":546,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":551,"modifier":"EXACT"},"end":{"value":558,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Turn","location":{"start":{"value":559,"modifier":"EXACT"},"end":{"value":561,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":563,"modifier":"EXACT"},"end":{"value":578,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":585,"modifier":"EXACT"},"end":{"value":588,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":591,"modifier":"EXACT"},"end":{"value":593,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":599,"modifier":"EXACT"},"end":{"value":610,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Turn","location":{"start":{"value":611,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":615,"modifier":"EXACT"},"end":{"value":631,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":638,"modifier":"EXACT"},"end":{"value":659,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Turn","location":{"start":{"value":660,"modifier":"EXACT"},"end":{"value":662,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":664,"modifier":"EXACT"},"end":{"value":670,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":674,"modifier":"EXACT"},"end":{"value":676,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":678,"modifier":"EXACT"},"end":{"value":680,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":682,"modifier":"EXACT"},"end":{"value":684,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Beta strand","location":{"start":{"value":692,"modifier":"EXACT"},"end":{"value":694,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":702,"modifier":"EXACT"},"end":{"value":708,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]},{"type":"Helix","location":{"start":{"value":710,"modifier":"EXACT"},"end":{"value":712,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4W8L"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"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-0677","category":"Domain","name":"Repeat"},{"id":"KW-0732","category":"Domain","name":"Signal"},{"id":"KW-0858","category":"Biological process","name":"Xylan degradation"}],"references":[{"referenceNumber":1,"citation":{"id":"10463183","citationType":"journal article","authors":["Blanco A.","Diaz P.","Zueco J.","Parascandola P.","Pastor F.I.J."],"citationCrossReferences":[{"database":"PubMed","id":"10463183"},{"database":"DOI","id":"10.1099/13500872-145-8-2163"}],"title":"A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes.","publicationDate":"1999","journal":"Microbiology","firstPage":"2163","lastPage":"2170","volume":"145"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","SUBSTRATE SPECIFICITY","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ006645","properties":[{"key":"ProteinId","value":"CAA07173.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T17628","properties":[{"key":"EntryName","value":"T17628"}]},{"database":"PDB","id":"4W8L","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.76 A"},{"key":"Chains","value":"A/B/C=367-718"}]},{"database":"PDB","id":"4XUN","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.75 A"},{"key":"Chains","value":"A/B/C=186-366"}]},{"database":"PDB","id":"4XUO","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A/B=29-186"}]},{"database":"PDB","id":"4XUP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.43 A"},{"key":"Chains","value":"A/B/C/D/E/F=28-361"}]},{"database":"PDB","id":"4XUQ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.95 A"},{"key":"Chains","value":"A/B/C=186-366"}]},{"database":"PDB","id":"4XUR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.67 A"},{"key":"Chains","value":"A/B/C=186-366"}]},{"database":"PDB","id":"4XUT","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A/B/C=186-366"}]},{"database":"AlphaFoldDB","id":"O69230","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"O69230","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O69230","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":"UniPathway","id":"UPA00114","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"O69230","properties":[{"key":"Description","value":"-"}]},{"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-EC"}]},{"database":"GO","id":"GO:0045493","properties":[{"key":"GoTerm","value":"P:xylan catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd00005","properties":[{"key":"EntryName","value":"CBM9_like_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00241","properties":[{"key":"EntryName","value":"DOMON_like"},{"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":"PANTHER","id":"PTHR31490:SF88","properties":[{"key":"EntryName","value":"BETA-XYLANASE"},{"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":"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"}]}],"sequence":{"value":"MRGKWLRLCLAAVLIVSLLPGLGAGEWKASAAKAGDILLSHSFEEGTTQGWTARGGVKVDVTAEQAYQGKQSLQTTGRTEAWNGPSLSLTDVVHKNEVVEISGYVKLVAGSAPPDLKFTVERRDRNGDTQYDQVNAAEQVTDQKWVKLQGQYSYEQGSSLLLYLESTDAKAAYLLDEFQIRLVKAAPENPGEPGEAGQALFKAYFEDGNIGNWRARGTEKLEVVSGIGHNSNRSLKTSSRSETYHGPLVEVLPYLQKGSTVHISFWAMYDEGPATQVINGSLEKEFNRDTANLEYAMFASTTLNKGQWKKIEADIIVPAESTGISGLRMYAETPWKQSSEVTETDTIPFYVDDVQITATEAIAIEKNIPDLAKKLGSSYALGAAIDQTALDPKDPHSELLTKHFNSITAGNFMKMDAMQPTEGKFVWSEADKLVNFAAANNMQVRGHTLLWHSQVPDWFFTDPNDPSKPATREQLMQRMKTHIQTIVSRYKGKVHTWDVVNEVISDGGGLRNQASGSKWRDIIGDVDGDGDDSDYIELAFRYAREADPDAVLVINDYGIEGSVSKMNDMVKLVEKLLAKGTPIDAIGFQMHVSMYGPDIKQIREAFNRAAALGVHIQVTELDMSIYSGNSEQEKPVTDEMMLEQAYRYRALFDLFKEFDDRGVMDSVTLWGLADDGTWLDDFPVKGRKDAPLLFDRKLKAKPAYWALVDPSTLPVYRNEWTASQAKVSLPDRKGQEDIIWGAVRALPFSHVIEGAVGTTGEVKTLWDGKQLNLRIEVKDATRLKGDQVEVFVSPEDMTAGKKNSTPKDGQYIFNRDGGKGKDQKLYQVKENKSGYVVYASLPLSSADLAAGKVLSLDFRITDKQPNGKTSIVVWNDVNNQQPQKTENRGKLKLGFDLKHAKVMYGTPTVDGKEDKLWKKAVTITTDVKVTGNSGAKAKAKLLWDEKYLYVLAEVKDPLLSKKSANAHEQDSIELFIDLNKNQTNSYEEDDAQYRVNFDNETSFGGSPRKELFKSATRLTKEGYIVEAAIPLENVRTKESKWIGFDLQVNDDGAGDGKRSSVFMWSDPSGNSYRDTSGFGSLLLMKK","length":1086,"molWeight":120586,"crc64":"4378361F1801A326","md5":"18DA6D7D06C5FB825A50DA4A61BFB9C5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":3,"Active site":3,"Beta strand":39,"Turn":5,"Helix":21},"uniParcId":"UPI00000B6C18"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"A0A0S2UQQ5","uniProtkbId":"REX8A_PAEBA","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-02-17","entryVersion":27,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"27316951"}],"value":"Reducing-end xylose-releasing exo-oligoxylanase Rex8A"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"27316951"}],"value":"Rex"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27316951"}],"value":"3.2.1.156"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"27316951"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"ALP73600.1"}],"value":"rex8A"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"PYE48000.1"}],"value":"DFQ00_11062"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27316951"}],"value":"Involved in depolymerization of xylan, a major component of the lignocellulosic substrates. Acts as an exo-oligoxylanase that efficiently hydrolyzes xylooligosaccharides, releasing xylose from their reducing ends. Hydrolyzes xylooligomers of 3 to 6 xylose units to xylose and xylobiose. Besides linear xylooligosaccharides, also hydrolyzes branched xylooligomers, such as xylooligomers decorated with 4-O-methyl-D-glucuronic acid moieties. Its proposed role is the degradation of xylooligomers produced by the activity of extracellular xylanases once they have been transported inside cells. Shows minor activity on polymeric xylan (glucuronoxylan from beechwood). Is not active on cellooligosaccharides or cellulosic substrates, or on other polysaccharides such as pectin, polygalacturonic acid, laminarin, or lichenan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides.","ecNumber":"3.2.1.156","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27316951"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":152.2,"unit":"umol/min/mg","enzyme":"enzyme for the hydrolysis of xylotriose","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27316951"}]}],"michaelisConstants":[{"constant":1.64,"unit":"mM","substrate":"xylotriose","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27316951"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27316951"}],"value":"kcat is 118.8 sec(-1) for the hydrolysis of xylotriose."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27316951"}],"value":"Optimum pH is 7 for the hydrolysis of xylotriose."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27316951"}],"value":"Optimum temperature is 40 degrees Celsius for the hydrolysis of xylotriose."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27316951"}],"value":"Glycan degradation; xylan degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 8 (cellulase D) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Reducing-end xylose-releasing exo-oligoxylanase Rex8A","featureId":"PRO_0000446222"},{"type":"Active site","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27316951"}]},{"type":"Active site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27316951"}]},{"type":"Mutagenesis","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"Loss of enzymatic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27316951"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Helix","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Turn","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Turn","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Turn","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Turn","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SHY"}]},{"type":"Beta strand","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Turn","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6TRH"}]},{"type":"Helix","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Turn","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Beta strand","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]},{"type":"Helix","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6SUD"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"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":"27316951","citationType":"journal article","authors":["Valenzuela S.V.","Lopez S.","Biely P.","Sanz-Aparicio J.","Pastor F.I."],"citationCrossReferences":[{"database":"PubMed","id":"27316951"},{"database":"DOI","id":"10.1128/aem.01329-16"}],"title":"The glycoside hydrolase family 8 reducing-end xylose-releasing exo-oligoxylanase Rex8A from Paenibacillus barcinonensis BP-23 is active on branched xylooligosaccharides.","publicationDate":"2016","journal":"Appl. Environ. Microbiol.","firstPage":"5116","lastPage":"5124","volume":"82"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBSTRATE SPECIFICITY","PATHWAY","3D-STRUCTURE MODELING","ACTIVE SITE","MUTAGENESIS OF GLU-70"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"26203337","citationType":"journal article","authors":["Whitman W.B.","Woyke T.","Klenk H.P.","Zhou Y.","Lilburn T.G.","Beck B.J.","De Vos P.","Vandamme P.","Eisen J.A.","Garrity G.","Hugenholtz P.","Kyrpides N.C."],"citationCrossReferences":[{"database":"PubMed","id":"26203337"},{"database":"DOI","id":"10.1186/s40793-015-0017-x"}],"title":"Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III: the genomes of soil and plant-associated and newly described type strains.","publicationDate":"2015","journal":"Stand. Genomic Sci.","firstPage":"26","lastPage":"26","volume":"10"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT251207","properties":[{"key":"ProteinId","value":"ALP73600.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"QJSW01000010","properties":[{"key":"ProteinId","value":"PYE48000.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110897543.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"PDB","id":"6SHY","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.81 A"},{"key":"Chains","value":"A/B=1-380"}]},{"database":"PDB","id":"6SRD","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.93 A"},{"key":"Chains","value":"A/B=1-380"}]},{"database":"PDB","id":"6SUD","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.74 A"},{"key":"Chains","value":"A/B=1-380"}]},{"database":"PDB","id":"6TO0","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.88 A"},{"key":"Chains","value":"A/B=1-380"}]},{"database":"PDB","id":"6TOW","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.05 A"},{"key":"Chains","value":"A/B=1-380"}]},{"database":"PDB","id":"6TPP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.64 A"},{"key":"Chains","value":"A/B=1-380"}]},{"database":"PDB","id":"6TRH","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.86 A"},{"key":"Chains","value":"A/B/C/D=1-380"}]},{"database":"AlphaFoldDB","id":"A0A0S2UQQ5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A0S2UQQ5","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GH8","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 8"}]},{"database":"OrthoDB","id":"9803461at2","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.2.1.156","properties":[{"key":"OrganismId","value":"13889"}]},{"database":"UniPathway","id":"UPA00114","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0033951","properties":[{"key":"GoTerm","value":"F:oligosaccharide reducing-end xylanase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"27316951"}]},{"database":"GO","id":"GO:0045493","properties":[{"key":"GoTerm","value":"P:xylan catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"27316951"}]},{"database":"Gene3D","id":"1.50.10.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008928","properties":[{"key":"EntryName","value":"6-hairpin_glycosidase_sf"}]},{"database":"InterPro","id":"IPR012341","properties":[{"key":"EntryName","value":"6hp_glycosidase-like_sf"}]},{"database":"InterPro","id":"IPR002037","properties":[{"key":"EntryName","value":"Glyco_hydro_8"}]},{"database":"Pfam","id":"PF01270","properties":[{"key":"EntryName","value":"Glyco_hydro_8"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00735","properties":[{"key":"EntryName","value":"GLHYDRLASE8"}]},{"database":"SUPFAM","id":"SSF48208","properties":[{"key":"EntryName","value":"Six-hairpin glycosidases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNITGKGAYDTGTYANLFQRSGYREDEIKARLEQTWNDLFYGDEHTRIYYPVGDDKGYMLDTGNDDVRSEGMSYGMMMAVQMDKKHEFDRLWNYAYTYMQHTEGRYKDYFAWHCKPDGTRLSPGPAPDGEEFFAMALFFASNRWGDGPAPYDYQAQARKILHACLHQGEQGEGDPMWEPSNRLIKFIPELPFSDPSYHLPHFYELFAQYANEQDRTFWKEAAEASRAYLRTACHPVTGLSPEYANYDGTPAPVQLHGDFRHFYSDAYRVAANVALDWEWFRKDPWQVQQSNRIQAFFSDIDVSDYRRYTIEGEPFNEPALHPVGLLATNAMASLAADGPDADSFVKRFWNTPLRQGKRRYYDNCLYFFTMLALSGNYRVY","length":380,"molWeight":44217,"crc64":"4AF704EE56FE61F9","md5":"E0421191C6E1DB642835D70A94699F6A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2,"Mutagenesis":1,"Helix":21,"Turn":6,"Beta strand":14},"uniParcId":"UPI0007224980"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"V9TSX0","uniProtkbId":"LPPX_PAEBA","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2014-03-19","entryVersion":29,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24549767"}],"value":"Chaperone protein LppX"}},"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24549767"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AHC74024.1"}],"value":"lppX"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"PYE48004.1"}],"value":"DFQ00_11066"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24549767"}],"value":"Is required for the expression of the adjacently encoded xylanase Xyn11E in an active form. LppX seems to act as a specific chaperone necessary for the correct folding of the xylanase during secretion across the cytoplasmic membrane"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}],"value":"Lipid-anchor","id":"SL-9901"}}]}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Chain","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"Chaperone protein LppX","featureId":"PRO_5016557793"},{"type":"Lipidation","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0564","category":"PTM","name":"Palmitate"},{"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"24549767","citationType":"journal article","authors":["Valenzuela S.V.","Diaz P.","Pastor F.I."],"citationCrossReferences":[{"database":"PubMed","id":"24549767"},{"database":"DOI","id":"10.1007/s00253-014-5565-2"}],"title":"Xyn11E from Paenibacillus barcinonensis BP-23: a LppX-chaperone-dependent xylanase with potential for upgrading paper pulps.","publicationDate":"2014","journal":"Appl. Microbiol. Biotechnol.","firstPage":"5949","lastPage":"5957","volume":"98"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"26203337","citationType":"journal article","authors":["Whitman W.B.","Woyke T.","Klenk H.P.","Zhou Y.","Lilburn T.G.","Beck B.J.","De Vos P.","Vandamme P.","Eisen J.A.","Garrity G.","Hugenholtz P.","Kyrpides N.C."],"citationCrossReferences":[{"database":"PubMed","id":"26203337"},{"database":"DOI","id":"10.1186/s40793-015-0017-x"}],"title":"Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III: the genomes of soil and plant-associated and newly described type strains.","publicationDate":"2015","journal":"Stand. Genomic Sci.","firstPage":"26","lastPage":"26","volume":"10"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KF766535","properties":[{"key":"ProteinId","value":"AHC74024.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"QJSW01000010","properties":[{"key":"ProteinId","value":"PYE48004.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110897547.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"V9TSX0","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"V9TSX0","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9768004at2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0120147","properties":[{"key":"GoTerm","value":"F:formylglycine-generating oxidase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044183","properties":[{"key":"GoTerm","value":"F:protein folding chaperone"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"24549767"}]},{"database":"GO","id":"GO:0006457","properties":[{"key":"GoTerm","value":"P:protein folding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"24549767"}]},{"database":"Gene3D","id":"3.90.1580.10","properties":[{"key":"EntryName","value":"paralog of FGE (formylglycine-generating enzyme)"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016187","properties":[{"key":"EntryName","value":"CTDL_fold"}]},{"database":"InterPro","id":"IPR051043","properties":[{"key":"EntryName","value":"Sulfatase_Mod_Factor_Kinase"}]},{"database":"InterPro","id":"IPR005532","properties":[{"key":"EntryName","value":"SUMF_dom"}]},{"database":"InterPro","id":"IPR042095","properties":[{"key":"EntryName","value":"SUMF_sf"}]},{"database":"PANTHER","id":"PTHR23150:SF19","properties":[{"key":"EntryName","value":"FORMYLGLYCINE-GENERATING ENZYME"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23150","properties":[{"key":"EntryName","value":"SULFATASE MODIFYING FACTOR 1, 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03781","properties":[{"key":"EntryName","value":"FGE-sulfatase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56436","properties":[{"key":"EntryName","value":"C-type lectin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRKWLIFLLIAAVAGLSACSTSGNTTVSDDLVLVEGGAFKTSKSSYSDKNVTLSDFYIGKYEVTQKQWMDVMGDNPSGFKGEERPVERVTWYDAIEYCNARSIKENLKPYYTIDKETTDPDNKNENDNIKWTVTINEGANGYRLPTGAEWEYAASGGQKSQNFTYSGSNNPDEVAWYWMNAGEKPLTGDWNWPAIENNRNQTKPVGQQKANELGIYDMSGNVREWCWEWHSHPETPENTWRISKGGGWVSSVNTAEISYPGKFDANGLGPDQGLRVVRSK","length":280,"molWeight":31488,"crc64":"11725ED3CAE6AE08","md5":"34C2F1B54A9E8DE2FD1D856428E80B3F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Lipidation":2},"uniParcId":"UPI0003D934FF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4URL1","uniProtkbId":"A0A2V4URL1_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-09-12","entryVersion":30,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57920.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase subunit PdxT"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"4.3.3.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pdx2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase glutaminase subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"3.5.1.2"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57920.1"}],"value":"pdxT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57920.1"}],"value":"HUB98_17510"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054599"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049534"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + phosphate + 3 H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31507"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58273"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:59776"},{"database":"ChEBI","id":"CHEBI:597326"}],"ecNumber":"4.3.3.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047992"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00064749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008345"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Belongs to the glutaminase PdxT/SNO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"value":"Belongs to the glutamine amidotransferase pdxT/SNO family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57920.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57920.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS57920.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110899499.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4URL1","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_17510","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9810320at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:1903600","properties":[{"key":"GoTerm","value":"C:glutaminase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036381","properties":[{"key":"GoTerm","value":"F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016740","properties":[{"key":"GoTerm","value":"F:transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006543","properties":[{"key":"GoTerm","value":"P:L-glutamine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042823","properties":[{"key":"GoTerm","value":"P:pyridoxal 5'-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008614","properties":[{"key":"GoTerm","value":"P:pyridoxine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01749","properties":[{"key":"EntryName","value":"GATase1_PB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000010","properties":[{"key":"EntryName","value":"uncharacterized protein LOC100176842 isoform X2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01615","properties":[{"key":"EntryName","value":"PdxT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR002161","properties":[{"key":"EntryName","value":"PdxT/SNO"}]},{"database":"InterPro","id":"IPR021196","properties":[{"key":"EntryName","value":"PdxT/SNO_CS"}]},{"database":"NCBIfam","id":"TIGR03800","properties":[{"key":"EntryName","value":"PLP_synth_Pdx2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559:SF0","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01174","properties":[{"key":"EntryName","value":"SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005639","properties":[{"key":"EntryName","value":"Glut_amidoT_SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01236","properties":[{"key":"EntryName","value":"PDXT_SNO_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51130","properties":[{"key":"EntryName","value":"PDXT_SNO_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKIGVLALQGAVTEHIRSIERAGAEGIAIKQVQQLEELDGLILPGGESTTIGKLMRKYGFMEAIRAFAAEGKPVFGTCAGLIVMAKHIHGQDEAHLELMDMTVSRNAFGRQRESFETDLPVKGIDETVRAVFIRAPLIESVGDGVEVLSTYNDEIVTARQGHLLACSYHPELTDDYRLHAYFVDMAKAYKQSVEAK","length":196,"molWeight":21548,"crc64":"EC7A64841DE4087F","md5":"BE107116C3BF6A4BECC0DD434D2412A5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":2},"countByFeatureType":{"Active site":5,"Binding site":3},"uniParcId":"UPI000D9773D1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4URN9","uniProtkbId":"A0A2V4URN9_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-09-12","entryVersion":29,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57948.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"6.3.4.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine 5'-triphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine triphosphate synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"UTP--ammonia ligase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"pyrG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57948.1"}],"value":"HUB98_17670"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":526,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":507,"modifier":"EXACT"},"end":{"value":507,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":509,"modifier":"EXACT"},"end":{"value":509,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":462,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57948.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57948.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS57948.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110899527.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4URN9","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_17670","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801107at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKYIFVTGGVVSSLGKGITAASLGRLLKNRGLKVTIQKFDPYINIDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDINLSKNSNVTTGKVYSSVISKERRGEYLGGTVQVIPHITNEIKERVFRAGREAGSDVVITEIGGTVGDIESLPFLEAIRQIKSDVGRDNVMYIHVTLIPYIKAAGEVKTKPTQHSVKELRSIGIQPNVIVCRTEYELSKDMKAKIALFCDIDENAVVECRDASTLYEVPLNLREEGLDEIVVNHLKLTTPAPDMSEWEGLVNRISKLERTVEIAIVGKYVALHDAYLSVVESLSHAGFASNADVKIRWVPSEDITDENVGDMLHGVGGILVPGGFGDRGIEGKVSAIRYAREKNIPFFGICLGMQVSVIEYARSIVGLNGANSSEINPATEFPVIDLLPEQKDIENLGGTMRLGLYPCKLQEGSLAMACYDDELVYERHRHRYEFNNEYREAIEKAGLVISGTSPDGRLVEIVELPGHPWFLAVQFHPEFTSRPNRPQPLFREFVKASLENAEK","length":534,"molWeight":59154,"crc64":"2FFC3AF8985FC370","md5":"A7D86EBB3C5E183D758735010824B85C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Region":1,"Active site":4,"Binding site":17},"uniParcId":"UPI000D9CBF61"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4V1E8","uniProtkbId":"A0A2V4V1E8_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-09-12","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58937.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Pyrimidine/purine nucleoside phosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"2.4.2.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"2.4.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Adenosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Cytidine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Guanosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Inosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Thymidine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Uridine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Xanthosine phosphorylase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"ppnP"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58937.1"}],"value":"HUB98_23775"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19805"},{"database":"ChEBI","id":"CHEBI:26386"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"},{"database":"ChEBI","id":"CHEBI:142355"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine + phosphate = alpha-D-ribose 1-phosphate + adenine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27642"},{"database":"ChEBI","id":"CHEBI:16335"},{"database":"ChEBI","id":"CHEBI:16708"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"cytidine + phosphate = cytosine + alpha-D-ribose 1-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:52540"},{"database":"ChEBI","id":"CHEBI:16040"},{"database":"ChEBI","id":"CHEBI:17562"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13233"},{"database":"ChEBI","id":"CHEBI:16235"},{"database":"ChEBI","id":"CHEBI:16750"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27646"},{"database":"ChEBI","id":"CHEBI:17368"},{"database":"ChEBI","id":"CHEBI:17596"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"thymidine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + thymine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16037"},{"database":"ChEBI","id":"CHEBI:17748"},{"database":"ChEBI","id":"CHEBI:17821"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57259"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uridine + phosphate = alpha-D-ribose 1-phosphate + uracil","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24388"},{"database":"ChEBI","id":"CHEBI:16704"},{"database":"ChEBI","id":"CHEBI:17568"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"xanthosine + phosphate = alpha-D-ribose 1-phosphate + xanthine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27638"},{"database":"ChEBI","id":"CHEBI:17712"},{"database":"ChEBI","id":"CHEBI:18107"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Belongs to the nucleoside phosphorylase PpnP family"}],"commentType":"SIMILARITY"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58937.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58937.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS58937.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110898659.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4V1E8","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_23775","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793848at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004731","properties":[{"key":"GoTerm","value":"F:purine-nucleoside phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016154","properties":[{"key":"GoTerm","value":"F:pyrimidine-nucleoside phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd20296","properties":[{"key":"EntryName","value":"cupin_PpnP-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.120.10:FF:000016","properties":[{"key":"EntryName","value":"Pyrimidine/purine nucleoside phosphorylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.10","properties":[{"key":"EntryName","value":"Jelly Rolls"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01537","properties":[{"key":"EntryName","value":"Nucleos_phosphorylase_PpnP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009664","properties":[{"key":"EntryName","value":"Ppnp"}]},{"database":"InterPro","id":"IPR014710","properties":[{"key":"EntryName","value":"RmlC-like_jellyroll"}]},{"database":"InterPro","id":"IPR011051","properties":[{"key":"EntryName","value":"RmlC_Cupin_sf"}]},{"database":"PANTHER","id":"PTHR36540","properties":[{"key":"EntryName","value":"PYRIMIDINE/PURINE NUCLEOSIDE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR36540:SF1","properties":[{"key":"EntryName","value":"PYRIMIDINE_PURINE NUCLEOSIDE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06865","properties":[{"key":"EntryName","value":"Ppnp"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51182","properties":[{"key":"EntryName","value":"RmlC-like cupins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSQFDQVSVVKKANIYYDGQVTSRTVILGDGSKVTLGIMLPGSYEFGTDSREIMEILSGDLKVLLPGEEEWQEIQGQATFHVPAESKFKLEIRSVTDYVCSYPAE","length":105,"molWeight":11697,"crc64":"10A9D0352B150BF5","md5":"D29F22EBB4B8012C4B5B0029BD0F8750"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":8,"SIMILARITY":1},"uniParcId":"UPI000D9E37F9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4V875","uniProtkbId":"A0A2V4V875_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-09-12","entryVersion":30,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57673.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Probable dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57673.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57673.1"}],"value":"HUB98_16105"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Region","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0698","category":"Biological process","name":"rRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57673.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57673.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS57673.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110897065.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4V875","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_16105","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793973at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000014","properties":[{"key":"EntryName","value":"Probable dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIKSSLYGLTLEQLRNWLPEHGQKKSRASRIWEWLYQERVHDFTGMSDVRQECLDVLSEHFTMNSLSEHVKQESSDGTVKFLLRLQDGNLIETVLMRQKYGLTVCVTTQVGCNIGCSFCASGLIKKSRDLSAGEIVEQIMHVQRHLDAAGQGELVTNVVVMGIGEPFDNFEHMSNFIEVIKDRKGLALAAKRITVSTSGLPDKIKEFADSSLQVNLAISLHAPNNELRTHIMKINRAFPIEQLMDAVDYYLEKTNKRIMFEYILLRDVNDQREHASELAELLSSRKSMVSVNLIPYNPVDEHSQYQRSTEESILGFYDTLKKNNINSTVRMEHGTDIDAACGQLRSKQMKNNAEAKANGKSDVKTDAGRLAMG","length":373,"molWeight":42142,"crc64":"112CC1FED36F2EB4","md5":"FE4252FC6791875615C534B5D9A0B811"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Active site":2,"Binding site":7},"uniParcId":"UPI000D92F8AD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4V9Q3","uniProtkbId":"A0A2V4V9Q3_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-09-12","entryVersion":29,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56199.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Probable dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56199.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56199.1"}],"value":"HUB98_07480"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0698","category":"Biological process","name":"rRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56199.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56199.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS56199.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110898582.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4V9Q3","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_07480","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793973at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000014","properties":[{"key":"EntryName","value":"Probable dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKPFIYDFSLEQLQQWAVENGEPAFRGGQIFDWIYVKRVNDFSEMTNLSKALREKLADQFEFVTLKEITKFESKDGTVKFLFGLHDDHAIETVIMKHNYGNSICVTTQVGCRIGCTFCASTLGGLKRNLTAGEIVAQVVQAQKILDERNERVSSIVIMGSGEPFENYEATMTFLRIMIHEKGLNIGQRHITVSTSGIVPNIYKFADEDTQINLAISIHAPNDALRSKLMPVNRRFPFEDVMESLRYYLAKTGRRITFEYALIGGVNDQPEHAAELASVLKNMLCHVNLIPVNHVPERKYVRTSRSDIFNFQRILSEQGVNVTIRREQGHDIAAACGQLRAKHMELR","length":346,"molWeight":39347,"crc64":"A747003B664C44E5","md5":"C6859246BA49622458BB35DB9B8DFA21"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7},"uniParcId":"UPI000D9CB43D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4VB60","uniProtkbId":"A0A2V4VB60_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-09-12","entryVersion":28,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55605.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein nucleotidyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein adenylyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.108"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein uridylyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.-"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"ydiU"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"selO"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55605.1"}],"value":"HUB98_04240"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Nucleotidyltransferase involved in the post-translational modification of proteins. It can catalyze the addition of adenosine monophosphate (AMP) or uridine monophosphate (UMP) to a protein, resulting in modifications known as AMPylation and UMPylation"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-[protein] + UTP = N(tele)-(5'-uridylyl)-L-histidyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83891"},{"database":"Rhea","id":"RHEA-COMP:9745"},{"database":"Rhea","id":"RHEA-COMP:20239"},{"database":"ChEBI","id":"CHEBI:29979"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:233474"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = 3-O-(5'-adenylyl)-L-seryl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58120"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:15073"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:142516"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + UTP = O-(5'-uridylyl)-L-seryl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:64604"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:16635"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:156051"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54292"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:13847"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:138113"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-(5'-adenylyl)-L-tyrosyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54288"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:13846"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:83624"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + UTP = O-(5'-uridylyl)-L-tyrosyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83887"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20238"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:90602"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009747"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Belongs to the SELO family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55605.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55605.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS55605.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110899323.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4VB60","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_04240","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9773505at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0070733","properties":[{"key":"GoTerm","value":"F:AMPylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_00692","properties":[{"key":"EntryName","value":"YdiU_SelO"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011009","properties":[{"key":"EntryName","value":"Kinase-like_dom_sf"}]},{"database":"InterPro","id":"IPR003846","properties":[{"key":"EntryName","value":"SelO"}]},{"database":"NCBIfam","id":"NF000658","properties":[{"key":"EntryName","value":"PRK00029.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32057","properties":[{"key":"EntryName","value":"PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32057:SF14","properties":[{"key":"EntryName","value":"PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02696","properties":[{"key":"EntryName","value":"SelO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56112","properties":[{"key":"EntryName","value":"Protein kinase-like (PK-like)"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEKKATAAGWNLEHSYAELPEAFYTSQNAVPVQSAELIIFNKALAASLGLQADALNNAEGAAIFAGNTMPEGAKPLAQAYAGHQFGNFNMLGDGRTLLLGEQITPQGERVDIQLKGSGRTPYSRGGDGRAAVGPMLREYIISEAMHGLGIPTTRSLAVVSTGEHIYRETERPGAILTRVAASHIRVATFQYAARWGAVADLRALADYTLQRHFPQIENDEQRYLRLLQEVIQLQAQLVSKWQCVGFIHGVMNTDNMAISGETIDYGPCAFMDTYHPATVFSSIDTQGRYAYGNQPYIAGWNLARFAETLLPLLHEDEEQAVQIAQDAIAQFSELYHQYWLKGMRAKLGLFSEETEDEVLVKDLLDLMEKHAVDYTNTFVSLTLGRWEGFTLKGHSDFDEWHSHWQARLGRQPESRDEVMQQMKRNNPVVIPRNERVEEVLERAEKDGDYSLIQPLLDMLQQPYAYTEEQQRYGVIPVSCDPSYKTFCGT","length":489,"molWeight":54835,"crc64":"869F0F2BBDDF3A96","md5":"3DB09828921D1A9DF0F09EBE26614AFF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"COFACTOR":1,"SIMILARITY":1},"countByFeatureType":{"Active site":1,"Binding site":11},"uniParcId":"UPI000D8D83F9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4VC25","uniProtkbId":"A0A2V4VC25_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-09-12","entryVersion":28,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS59843.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01400"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}],"value":"Multifunctional fusion protein"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}],"value":"Peptide methionine sulfoxide reductase MsrA"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}],"value":"Protein-methionine-S-oxide reductase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}],"value":"1.8.4.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}],"value":"Peptide-methionine (S)-S-oxide reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}],"value":"Peptide Met(O) reductase"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01400"}],"value":"Peptide methionine sulfoxide reductase MsrB"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01400"}],"value":"1.8.4.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01400"}],"value":"Peptide-methionine (R)-S-oxide reductase"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01400"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS59843.1"}],"value":"msrB"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}],"value":"msrA"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS59843.1"}],"value":"HUB98_28980"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}],"value":"Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L-methionyl-(R)-S-oxide-[protein] + [thioredoxin]-dithiol","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24164"},{"database":"Rhea","id":"RHEA-COMP:10698"},{"database":"Rhea","id":"RHEA-COMP:10700"},{"database":"Rhea","id":"RHEA-COMP:12313"},{"database":"Rhea","id":"RHEA-COMP:12314"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16044"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:45764"},{"database":"ChEBI","id":"CHEBI:50058"}],"ecNumber":"1.8.4.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048488"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01400"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L-methionyl-(S)-S-oxide-[protein] + [thioredoxin]-dithiol","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14217"},{"database":"Rhea","id":"RHEA-COMP:10698"},{"database":"Rhea","id":"RHEA-COMP:10700"},{"database":"Rhea","id":"RHEA-COMP:12313"},{"database":"Rhea","id":"RHEA-COMP:12315"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16044"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:44120"},{"database":"ChEBI","id":"CHEBI:50058"}],"ecNumber":"1.8.4.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047806"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[thioredoxin]-disulfide + L-methionine + H2O = L-methionine (S)-S-oxide + [thioredoxin]-dithiol","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19993"},{"database":"Rhea","id":"RHEA-COMP:10698"},{"database":"Rhea","id":"RHEA-COMP:10700"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:50058"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:58772"}],"ecNumber":"1.8.4.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048782"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}],"value":"Belongs to the MsrA Met sulfoxide reductase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007174"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01400"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01126"}],"value":"Belongs to the MsrB Met sulfoxide reductase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008076"}],"value":"In the C-terminal section; belongs to the MsrB Met sulfoxide reductase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011017"}],"value":"In the N-terminal section; belongs to the MsrA Met sulfoxide reductase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01400"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01126"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":360,"modifier":"EXACT"}},"description":"Multifunctional fusion protein","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5048454495"},{"type":"Domain","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"MsrB","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51790"}]},{"type":"Active site","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01401"}]},{"type":"Active site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01400"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01126"}]},{"type":"Lipidation","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"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":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01400"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0564","category":"PTM","name":"Palmitate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"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":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS59843.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS59843.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS59843.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110895964.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4VC25","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_28980","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"4174719at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0033743","properties":[{"key":"GoTerm","value":"F:peptide-methionine (R)-S-oxide reductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008113","properties":[{"key":"GoTerm","value":"F:peptide-methionine (S)-S-oxide reductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030091","properties":[{"key":"GoTerm","value":"P:protein repair"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006979","properties":[{"key":"GoTerm","value":"P:response to oxidative stress"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"2.170.150.20:FF:000003","properties":[{"key":"EntryName","value":"Peptide methionine sulfoxide reductase MsrB"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.170.150.20","properties":[{"key":"EntryName","value":"Peptide methionine sulfoxide reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1060.10","properties":[{"key":"EntryName","value":"Peptide methionine sulphoxide reductase MsrA"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01401","properties":[{"key":"EntryName","value":"MsrA"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01400","properties":[{"key":"EntryName","value":"MsrB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002569","properties":[{"key":"EntryName","value":"Met_Sox_Rdtase_MsrA_dom"}]},{"database":"InterPro","id":"IPR036509","properties":[{"key":"EntryName","value":"Met_Sox_Rdtase_MsrA_sf"}]},{"database":"InterPro","id":"IPR028427","properties":[{"key":"EntryName","value":"Met_Sox_Rdtase_MsrB"}]},{"database":"InterPro","id":"IPR002579","properties":[{"key":"EntryName","value":"Met_Sox_Rdtase_MsrB_dom"}]},{"database":"InterPro","id":"IPR011057","properties":[{"key":"EntryName","value":"Mss4-like_sf"}]},{"database":"NCBIfam","id":"TIGR00401","properties":[{"key":"EntryName","value":"msrA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00357","properties":[{"key":"EntryName","value":"peptide-methionine (R)-S-oxide reductase MsrB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10173","properties":[{"key":"EntryName","value":"METHIONINE SULFOXIDE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10173:SF59","properties":[{"key":"EntryName","value":"PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA_MSRB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01625","properties":[{"key":"EntryName","value":"PMSR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01641","properties":[{"key":"EntryName","value":"SelR"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51316","properties":[{"key":"EntryName","value":"Mss4-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55068","properties":[{"key":"EntryName","value":"Peptide methionine sulfoxide reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51790","properties":[{"key":"EntryName","value":"MSRB"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKGPWLGLCLLTIALIVSACGAKMEPRSASAPAQAVQISNIPDEELRDLYLAGGCFWGVEAYMARILGVQDVTSGYANGEGENPTYEDVIRGDRGFAETVHVKYDPRQVSLQKLLEAYFRVIDPTSLNKQGNDRGIQYRTGIYYSSPEDETVIQQAVAKEQTHYKQPIVTEVMPLENYYLAEEYHQDYLEKNPNGYCHIDMSVLDEQEIVIDPAQYPRPTDEQLQKQLTDEQYAVAVNNDTEHAFSNEYWDNEQPGLYVDIATGEPLFSSRDKYDSGCGWPSFTRPIVPEVVTYKQDTSFGMERTEVRSRAGDIHLGHVFDDGPQDRGGKRYCINSASIRFVPLDQMGQERYGYLLSLIE","length":360,"molWeight":40718,"crc64":"93EC275AE267EEFA","md5":"099DF6E0CEE8FD24343E171BA3F6B658"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1,"Active site":2,"Lipidation":2},"uniParcId":"UPI000D807215"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4VDM8","uniProtkbId":"A0A2V4VDM8_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-09-12","entryVersion":35,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56040.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Riboflavin biosynthesis protein RibBA"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3,4-dihydroxy-2-butanone 4-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"DHBP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"4.1.99.12"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase-2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3.5.4.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase II"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"ribBA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56040.1"}],"value":"HUB98_06575"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002284"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043932"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18457"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:58121"},{"database":"ChEBI","id":"CHEBI:58830"}],"ecNumber":"4.1.99.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 2 phosphate + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23704"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58614"}],"ecNumber":"3.5.4.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049295"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Binds 2 divalent metal cations per subunit. Magnesium or manganese."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004904"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004853"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the C-terminal section; belongs to the GTP cyclohydrolase II family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005520"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the N-terminal section; belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00925"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"DHBP synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Region","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"Proton acceptor; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"Nucleophile; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Binding site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Site","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022619"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0686","category":"Biological process","name":"Riboflavin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56040.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56040.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS56040.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110895186.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4VDM8","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_06575","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793111at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008686","properties":[{"key":"GoTerm","value":"F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003935","properties":[{"key":"GoTerm","value":"F:GTP cyclohydrolase II activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00641","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10990:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.870.10:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.870.10","properties":[{"key":"EntryName","value":"DHBP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10990","properties":[{"key":"EntryName","value":"GTP cyclohydrolase II"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00179","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00180","properties":[{"key":"EntryName","value":"RibB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01283","properties":[{"key":"EntryName","value":"RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017945","properties":[{"key":"EntryName","value":"DHBP_synth_RibB-like_a/b_dom"}]},{"database":"InterPro","id":"IPR000422","properties":[{"key":"EntryName","value":"DHBP_synthase_RibB"}]},{"database":"InterPro","id":"IPR032677","properties":[{"key":"EntryName","value":"GTP_cyclohydro_II"}]},{"database":"InterPro","id":"IPR000926","properties":[{"key":"EntryName","value":"RibA"}]},{"database":"InterPro","id":"IPR036144","properties":[{"key":"EntryName","value":"RibA-like_sf"}]},{"database":"InterPro","id":"IPR016299","properties":[{"key":"EntryName","value":"Riboflavin_synth_RibBA"}]},{"database":"NCBIfam","id":"NF006803","properties":[{"key":"EntryName","value":"PRK09311.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001591","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00505","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00506","properties":[{"key":"EntryName","value":"ribB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327:SF18","properties":[{"key":"EntryName","value":"3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE II-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00926","properties":[{"key":"EntryName","value":"DHBP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00925","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001259","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF142695","properties":[{"key":"EntryName","value":"RibA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55821","properties":[{"key":"EntryName","value":"YrdC/RibB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSEQAEPSVLDSIEEAIYDLMRGKPVIVVDDEDRENEGDFIALAEKATPEVINFMITEGRGLVCVPITQQRADELNLKPMVQQNTDFHGTAFTVSVDHTDTTTGISAHERSITVKGLIDPNAKSNDFRKPGHMFPLIAKDGGVLRRAGHTEAAVDLAIMCGSYPAGVICEVIKEDGTMARLPDLQEIARKHNLKLISIQDMIRYRNEKEQLVQREVSVRMPTDFGEFQAVAYTNAVDNKEHIALVKGEIDGSKPVLVRVHSECLTGDVFHSHRCDCGPQFDAALKQIHEEGNGVLLYMRQEGRGIGLINKLKAYKLQEEGLDTVEANQKLGFAADLRDYGIGAQILKDLGVRQIRLLTNNPRKIKGLEGYGLEVVERVPIQMKENADNTAYLHTKQAKLGHMLKFDDIEQNEQ","length":413,"molWeight":45995,"crc64":"BC401C9667208BAA","md5":"22415C065630D533A03BE5D289247499"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":3,"PATHWAY":2,"SIMILARITY":2},"countByFeatureType":{"Domain":1,"Region":2,"Active site":2,"Binding site":16,"Site":2},"uniParcId":"UPI000D812589"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4VEY3","uniProtkbId":"A0A2V4VEY3_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-09-12","entryVersion":30,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS59507.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphohexokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS59507.1"}],"value":"pfkA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS59507.1"}],"value":"HUB98_27065"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002659"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16109"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS59507.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS59507.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS59507.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110893462.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4VEY3","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_27065","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802503at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.50.450:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00339","properties":[{"key":"EntryName","value":"Phosphofructokinase_I_B1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR012003","properties":[{"key":"EntryName","value":"ATP_PFK_prok-type"}]},{"database":"InterPro","id":"IPR012828","properties":[{"key":"EntryName","value":"PFKA_ATP_prok"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02482","properties":[{"key":"EntryName","value":"PFKA_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002872","properties":[{"key":"EntryName","value":"PRK03202.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF4","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000532","properties":[{"key":"EntryName","value":"ATP_PFK_prok"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAVKKIAVLTSGGDSQGMNAAVRAVVRSGLYHGLEVFGIQRGYQGLLNNDIFPMDLRSVGDIIQRGGTVLQSARCKEFYTAEGQQKGADILRARGIDGLIVIGGDGSYNGANKLSKLGINTMGLPGTIDNDISFTDYTIGFDTSVSVVVDAVNKLRDTMSSHERSSIVEVMGRHCGDIALHAGLASGAETILVPEVPFDMDEVAERMKANFAHGKRHSIIIVAEGVGKGEDVAKELMERCPTYEPRVTVLGHIQRGGTPTPFDRNLASRLGDFAVRSLIAGETDKGCGIIKGELVLTDIDKVVNTKKAFDMETYELAQRLSQ","length":323,"molWeight":34674,"crc64":"EFE5DD87542A49BC","md5":"2F15B80306BFFFF3E6ED0E546F8C3BA8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":14},"uniParcId":"UPI000D9C29A7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4VHS6","uniProtkbId":"A0A2V4VHS6_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-09-12","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56203.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56203.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56203.1"}],"value":"HUB98_07505"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19397"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"6.3.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (R)-4'-phosphopantetheine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16793"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"4.1.1.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Binds 1 FMN per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the C-terminal section; belongs to the PPC synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"DNA/pantothenate metabolism flavoprotein C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04127"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Active site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56203.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56203.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS56203.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110898578.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4VHS6","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_07505","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802554at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0071513","properties":[{"key":"GoTerm","value":"C:phosphopantothenoylcysteine decarboxylase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004632","properties":[{"key":"GoTerm","value":"F:phosphopantothenate--cysteine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004633","properties":[{"key":"GoTerm","value":"F:phosphopantothenoylcysteine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015941","properties":[{"key":"GoTerm","value":"P:pantothenate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.10300","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1950","properties":[{"key":"EntryName","value":"Flavin prenyltransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02225","properties":[{"key":"EntryName","value":"CoaBC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR035929","properties":[{"key":"EntryName","value":"CoaB-like_sf"}]},{"database":"InterPro","id":"IPR005252","properties":[{"key":"EntryName","value":"CoaBC"}]},{"database":"InterPro","id":"IPR007085","properties":[{"key":"EntryName","value":"DNA/pantothenate-metab_flavo_C"}]},{"database":"InterPro","id":"IPR036551","properties":[{"key":"EntryName","value":"Flavin_trans-like"}]},{"database":"InterPro","id":"IPR003382","properties":[{"key":"EntryName","value":"Flavoprotein"}]},{"database":"NCBIfam","id":"TIGR00521","properties":[{"key":"EntryName","value":"coaBC_dfp"},{"key":"MatchStatus","value":"2"}]},{"database":"PANTHER","id":"PTHR14359","properties":[{"key":"EntryName","value":"HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359:SF6","properties":[{"key":"EntryName","value":"PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04127","properties":[{"key":"EntryName","value":"DFP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02441","properties":[{"key":"EntryName","value":"Flavoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102645","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52507","properties":[{"key":"EntryName","value":"Homo-oligomeric flavin-containing Cys decarboxylases, HFCD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLNGKRIVLGVTGGIAAYKAATLCSKLVQKGADVHVIMTSSATQFITELTLQTLTRNPVYTDTFDEREPAVVSHIHLADLADLVLVAPATANVIAKMAHGMADDMLTTTLLATTAPVMVAPAMNVHMYDHPAVKQNMNVLVERGTLMIEPGEGLLACGYVGKGRLEEPETIVDVVERFFTQRNAASMQRAGQGWTNVQTQTQGQELLLKGKKVVVTAGGTVERIDPVRYITNDSSGKMGFAIAAAARDLGAEVKLVMGNTQAQPPEQVEVIPVQSAQEMYEAVSSEWNDADIVIKAAAVADYRPKEVYTEKIKKKGDTLSLELVKNIDILETLGKRKTHQYLIGFAAETQSLEMHAREKLERKNCDLIVANDVTRSGAGFGTDTNAVHIYDRDGLVEELELMSKQDVAHRLLRIAAERIAGRN","length":423,"molWeight":46036,"crc64":"ECCC22AA2EC2D70B","md5":"C7C22E5F810A81B00F48AC53994490D9"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":5},"uniParcId":"UPI000D9BDA3C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4VI36","uniProtkbId":"A0A2V4VI36_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-09-12","entryVersion":31,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56285.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthetase ammonia chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56285.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56285.1"}],"value":"HUB98_07995"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060037"}],"value":"Small subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of the biosynthetic pathway leading to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"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. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":680,"modifier":"EXACT"},"end":{"value":870,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":939,"modifier":"EXACT"},"end":{"value":1071,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":556,"modifier":"EXACT"},"end":{"value":938,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":939,"modifier":"EXACT"},"end":{"value":1071,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":716,"modifier":"EXACT"},"end":{"value":716,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":755,"modifier":"EXACT"},"end":{"value":755,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":761,"modifier":"EXACT"},"end":{"value":761,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":786,"modifier":"EXACT"},"end":{"value":786,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":787,"modifier":"EXACT"},"end":{"value":787,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":788,"modifier":"EXACT"},"end":{"value":788,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":789,"modifier":"EXACT"},"end":{"value":789,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":829,"modifier":"EXACT"},"end":{"value":829,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":829,"modifier":"EXACT"},"end":{"value":829,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":829,"modifier":"EXACT"},"end":{"value":829,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"3"}},{"type":"Binding site","location":{"start":{"value":841,"modifier":"EXACT"},"end":{"value":841,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":841,"modifier":"EXACT"},"end":{"value":841,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":841,"modifier":"EXACT"},"end":{"value":841,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"4"}},{"type":"Binding site","location":{"start":{"value":841,"modifier":"EXACT"},"end":{"value":841,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"3"}},{"type":"Binding site","location":{"start":{"value":841,"modifier":"EXACT"},"end":{"value":841,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}},{"type":"Binding site","location":{"start":{"value":843,"modifier":"EXACT"},"end":{"value":843,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"4"}},{"type":"Binding site","location":{"start":{"value":843,"modifier":"EXACT"},"end":{"value":843,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56285.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS56285.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS56285.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110898481.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4VI36","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_07995","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804197at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.1490.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000026","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_A","properties":[{"key":"EntryName","value":"CPSase_L_chain_A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPINKDLKKILVIGSGPIVIGQAAEFDYAGTQACQALKEEGVEVVLINSNPATIMTDTNMADKVYIEPITLDFVTQIIRQERPDGLLPTLGGQTGLNMAVELARAGVLERENVKLLGTQLTSIEKAEDRDLFRDLMRELEQPVPESVIVTTLEESLQFAGEIGYPIIVRPAYTLGGTGGGICANEEELRETVAAGIRYSPIGQCLVEKSIAGMKEVEYEVMRDKNDNCIVVCNMENFDPVGVHTGDSIVVAPSQTLSDREYQMLRSASLKIIRALNIEGGCNVQFALDPHSFQYYVIEVNPRVSRSSALASKATGYPIAKMAAKIAMGYTLDEIVNPVTGQTYACFEPTLDYIVSKIPRWPFDKFTSANRKLGTQMKATGEVMAIGRTFEESIHKAVRSLEIGVHRLYLKGAEMLDEETLNERLVKADDERMFLIAEAFRRGYTLQQLQDLTKIDWWFLDKIEGLIQFEDRVRAESELTSETLYQAKRLGFTDRAIAELRAEGQPGGTLTTEAEVRARREEENLRPVYKMVDTCAAEFEATTPYYYSTYETENEVLPSDKKKVVVLGSGPIRIGQGIEFDYSTVHAVWALQKAGYEAVIINNNPETVSTDFNTSDRLYFEPLFFEDVMNVIEQEQPVGVIVQFGGQTAINLAAPLRNAGVTILGTDLESIDEAEDRKKFERLLSRLEIAQPKGKTVISVDDAVETAQSLGYPVLVRPSYVLGGRAMEIVYSDAELLTYMEQAVKINPEHPVLIDRYMLGKEVEVDAICDGETVLVPGIMEHIERAGVHSGDSIAVYPPQHLSADLKEKIVEITIKIAKELKTVGLVNIQFVIHEGQVYVIEVNPRSSRTVPFLSKVTNIPMANLATQAILGVKLKELGYVDGLWPETDHVSVKVPVFSFAKLRRVEPTLGPEMKSTGEVMGRDPNYAKALFKGLIGAGMKIPATGAIVVTVADKDKDEAVPLLEGFYRLGYKIMATGGTAAALQAANIPVTVVNKLSEGSPNILDMIRSGEANFVFNTLTKGKTPQRDGFRIRREAVENGVVCMTSLDTIRALLIMLQTINFSSEAMPAFV","length":1071,"molWeight":118208,"crc64":"78AE4D515A9C9008","md5":"E13FB8BDF37AE31BBFF9885B3595E6EA"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":3,"Binding site":37},"uniParcId":"UPI000D893C14"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4VIX4","uniProtkbId":"A0A2V4VIX4_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-09-12","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55329.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate dehydrogenase [ubiquinone]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"1.2.5.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate oxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"POX"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate:ubiquinone-8 oxidoreductase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55329.1"}],"value":"poxB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55329.1"}],"value":"HUB98_02720"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO(2). It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a ubiquinone + pyruvate + H2O = a ubiquinol + acetate + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27405"},{"database":"Rhea","id":"RHEA-COMP:9565"},{"database":"Rhea","id":"RHEA-COMP:9566"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16389"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:17976"},{"database":"ChEBI","id":"CHEBI:30089"}],"ecNumber":"1.2.5.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 FAD per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"thiamine diphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58937"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 thiamine pyrophosphate per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"The C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Has 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region. The C-terminus is held closely against the rest of the protein and covers the active site; during activation it unfolds from the rest of the protein and forms an amphipathic helix upon membrane binding, exposing the active site"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362132"}],"value":"Belongs to the TPP enzyme family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme N-terminal TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02776"}]},{"type":"Domain","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00205"}]},{"type":"Domain","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":527,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02775"}]},{"type":"Region","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"FAD-binding domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]},{"type":"Region","location":{"start":{"value":534,"modifier":"EXACT"},"end":{"value":575,"modifier":"EXACT"}},"description":"Membrane-binding domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":436,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":463,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Site","location":{"start":{"value":468,"modifier":"EXACT"},"end":{"value":468,"modifier":"EXACT"}},"description":"Moves into active site upon enzyme activation, plays a role in electron transfer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0446","category":"Ligand","name":"Lipid-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55329.1"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55329.1"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023052"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0786","category":"Ligand","name":"Thiamine pyrophosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55329.1"}],"id":"KW-0830","category":"Ligand","name":"Ubiquinone"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55329.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS55329.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS55329.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110896623.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4VIX4","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_02720","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"4494979at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008289","properties":[{"key":"GoTerm","value":"F:lipid binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052737","properties":[{"key":"GoTerm","value":"F:pyruvate dehydrogenase (quinone) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030976","properties":[{"key":"GoTerm","value":"F:thiamine pyrophosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048039","properties":[{"key":"GoTerm","value":"F:ubiquinone binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042867","properties":[{"key":"GoTerm","value":"P:pyruvate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02014","properties":[{"key":"EntryName","value":"TPP_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07039","properties":[{"key":"EntryName","value":"TPP_PYR_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1220:FF:000013","properties":[{"key":"EntryName","value":"Pyruvate dehydrogenase [ubiquinone]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.1220","properties":[{"key":"EntryName","value":"TPP-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00850","properties":[{"key":"EntryName","value":"POX"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029035","properties":[{"key":"EntryName","value":"DHS-like_NAD/FAD-binding_dom"}]},{"database":"InterPro","id":"IPR047211","properties":[{"key":"EntryName","value":"POXB-like"}]},{"database":"InterPro","id":"IPR044261","properties":[{"key":"EntryName","value":"Pyruvate_dehydrogenase"}]},{"database":"InterPro","id":"IPR029061","properties":[{"key":"EntryName","value":"THDP-binding"}]},{"database":"InterPro","id":"IPR012000","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_cen_dom"}]},{"database":"InterPro","id":"IPR012001","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_TPP-bd_dom"}]},{"database":"InterPro","id":"IPR000399","properties":[{"key":"EntryName","value":"TPP-bd_CS"}]},{"database":"InterPro","id":"IPR011766","properties":[{"key":"EntryName","value":"TPP_enzyme_TPP-bd"}]},{"database":"InterPro","id":"IPR047212","properties":[{"key":"EntryName","value":"TPP_POXB-like"}]},{"database":"InterPro","id":"IPR047210","properties":[{"key":"EntryName","value":"TPP_PYR_POXB-like"}]},{"database":"NCBIfam","id":"NF006591","properties":[{"key":"EntryName","value":"poxB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981:SF2","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02775","properties":[{"key":"EntryName","value":"TPP_enzyme_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00205","properties":[{"key":"EntryName","value":"TPP_enzyme_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02776","properties":[{"key":"EntryName","value":"TPP_enzyme_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52467","properties":[{"key":"EntryName","value":"DHS-like NAD/FAD-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52518","properties":[{"key":"EntryName","value":"Thiamin diphosphate-binding fold (THDP-binding)"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00187","properties":[{"key":"EntryName","value":"TPP_ENZYMES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKTIADVLVEALLNAGIKRIYGIVGDSLNAVLDSIRRSGKIEWIHVRHEEVAAFAAGADAQVSGSIAVCAGSSGPGNMHLINGLYDCHRNRVPVLAIAAHIPSDEIGSEYFQATHPEYLFQECSHYCEVITTAKQMPRSVTMAMQTAVARSGVSVIVLPGDVAGLEAADLPVPEHVYHAPHPVVHPSEPELAKLAEYLNEDKKITLLCGAGCAGAREPLLELCDRLKAPMVIALRGKEYLEYDNPYSVGLTGLIGYSSGYHAMMDCDVLLMLGTDFPYRQFYPEDATVLQVDIQTSHLGRRTKLDYGVCGDVKATLEALLPHLTAEHSDKHLRKSVKHYTKVREELDELAVGKPGKKPIHPQYLTKVISDAAAENAIFTCDVGTPTVWAARYVEMSQSRRLLGSFNHGTMANALPQAIGAQVANPGRQVISLSGDGGLAMLMGDLLTLKQHKLPVKVVVFNNGALSFVELEMKAAGFLESGTELVNPNFAMVAQAMGIEGIRVEDPEELEGAIERALLHDGPVLIDAVVNRQELSLPPKINLKQAEGFTLWMMKAVLNGRGDELIELAKTNLFR","length":575,"molWeight":62433,"crc64":"4CDCC375F76DCF82","md5":"B85DCD676C538ECC0D82A23B45E1033C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":3,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":2,"Binding site":9,"Site":1},"uniParcId":"UPI000D94B168"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4VJ39","uniProtkbId":"A0A2V4VJ39_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2018-09-12","entryVersion":32,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57185.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00016090"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"Glutamine--fructose-6-phosphate aminotransferase [isomerizing]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012916"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"2.6.1.16"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"D-fructose-6-phosphate amidotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"GFAT"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"Glucosamine-6-phosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"Hexosephosphate aminotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"L-glutamine--D-fructose-6-phosphate amidotransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57185.1"}],"value":"glmS"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57185.1"}],"value":"HUB98_13245"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13237"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:58725"},{"database":"ChEBI","id":"CHEBI:61527"}],"ecNumber":"2.6.1.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001031"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"Cytoplasm","id":"SL-0086"}}]}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}]},{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"Glutamine amidotransferase type-2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51278"}]},{"type":"Domain","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":425,"modifier":"EXACT"}},"description":"SIS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51464"}]},{"type":"Domain","location":{"start":{"value":458,"modifier":"EXACT"},"end":{"value":600,"modifier":"EXACT"}},"description":"SIS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51464"}]},{"type":"Region","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00609"}]},{"type":"Active site","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"Nucleophile; for GATase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}]},{"type":"Active site","location":{"start":{"value":605,"modifier":"EXACT"},"end":{"value":605,"modifier":"EXACT"}},"description":"For Fru-6P isomerization activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022576"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"id":"KW-0032","category":"Molecular function","name":"Aminotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00797"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00609"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57185.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS57185.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS57185.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110899674.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4VJ39","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_13245","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"106547at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030246","properties":[{"key":"GoTerm","value":"F:carbohydrate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0097367","properties":[{"key":"GoTerm","value":"F:carbohydrate derivative binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004360","properties":[{"key":"GoTerm","value":"F:L-glutamine:D-fructose-6-phosphate transaminase (isomerizing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006487","properties":[{"key":"GoTerm","value":"P:protein N-linked glycosylation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006047","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00714","properties":[{"key":"EntryName","value":"GFAT"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05008","properties":[{"key":"EntryName","value":"SIS_GlmS_GlmD_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05009","properties":[{"key":"EntryName","value":"SIS_GlmS_GlmD_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10490:FF:000001","properties":[{"key":"EntryName","value":"Glutamine--fructose-6-phosphate aminotransferase [isomerizing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10490:FF:000022","properties":[{"key":"EntryName","value":"Glutamine--fructose-6-phosphate aminotransferase [isomerizing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.60.20.10:FF:000006","properties":[{"key":"EntryName","value":"Glutamine--fructose-6-phosphate aminotransferase [isomerizing]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10490","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase like protein, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.60.20.10","properties":[{"key":"EntryName","value":"Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00164","properties":[{"key":"EntryName","value":"GlmS"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017932","properties":[{"key":"EntryName","value":"GATase_2_dom"}]},{"database":"InterPro","id":"IPR005855","properties":[{"key":"EntryName","value":"GFAT"}]},{"database":"InterPro","id":"IPR047084","properties":[{"key":"EntryName","value":"GFAT_N"}]},{"database":"InterPro","id":"IPR035466","properties":[{"key":"EntryName","value":"GlmS/AgaS_SIS"}]},{"database":"InterPro","id":"IPR035490","properties":[{"key":"EntryName","value":"GlmS/FrlB_SIS"}]},{"database":"InterPro","id":"IPR029055","properties":[{"key":"EntryName","value":"Ntn_hydrolases_N"}]},{"database":"InterPro","id":"IPR001347","properties":[{"key":"EntryName","value":"SIS_dom"}]},{"database":"InterPro","id":"IPR046348","properties":[{"key":"EntryName","value":"SIS_dom_sf"}]},{"database":"NCBIfam","id":"TIGR01135","properties":[{"key":"EntryName","value":"glmS"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001484","properties":[{"key":"EntryName","value":"PRK00331.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10937","properties":[{"key":"EntryName","value":"GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10937:SF0","properties":[{"key":"EntryName","value":"GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING)"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13537","properties":[{"key":"EntryName","value":"GATase_7"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01380","properties":[{"key":"EntryName","value":"SIS"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF56235","properties":[{"key":"EntryName","value":"N-terminal nucleophile aminohydrolases (Ntn hydrolases)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53697","properties":[{"key":"EntryName","value":"SIS domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51278","properties":[{"key":"EntryName","value":"GATASE_TYPE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51464","properties":[{"key":"EntryName","value":"SIS"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MCGIVGYIGNKNTQSVLIEGLKKLEYRGYDSAGIAVFTPQGLQITKALGRLANLEAKLDGAPLVGNAGIGHTRWATHGKPSDENSHPHTDESQKFSVVHNGIIENYLELKDELIAEGHTFSSETDTEVISHLIAREYNGDIVKAVQKVITLMRGAFALGVLTEYEPEKLVAVRQASPLIIGIGEGENFIGSDIPAILEHTRNVYILNDGEMAVLTHDAVELMTIEGNFISREMIHVDWDAVTAEKGGFEHFMLKEIHEQPKAYRDTMLGRIDNEGRKVQLPELKMTEEQIKNIRNIQIIACGTAYHAGLVGRTVIEQLVRIPVETDVASEYRYRSPIVNKDTLVIVVSQSGETADTLAALREAQSNGAHVLAITNVVGSSIARDANDVIATLAGPEIAVASTKAYTSQLIAFNLLGLYLAQVRGTKTPDEIAHTLAAMQALPEQVESMLEQADAIKGYAEQISKHQHLFFIGRGLDYAVAQEGSLKLKEISYIHSEAYAAGELKHGTLALIEDGIPVIALATQENVLEKTVSNIKEVKARGADVLAITYEEHVAPLLKSVDQAFAIPKTLPLLSPALSVVALQLLAYYASLALGHDVDKPRNLAKSVTVE","length":610,"molWeight":66291,"crc64":"695593EF39E9920E","md5":"08375FA879002D1F170236AD4B85E555"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1},"countByFeatureType":{"Initiator methionine":1,"Domain":3,"Region":1,"Compositional bias":1,"Active site":3},"uniParcId":"UPI000D83821D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4WIX4","uniProtkbId":"A0A2V4WIX4_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-09-12","entryVersion":31,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60403.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Dihydroorotate dehydrogenase (quinone)"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"1.3.5.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"DHOdehase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"DHOD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"DHODase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Dihydroorotate oxidase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"pyrD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60403.1"}],"value":"HUB98_27180"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003616"}],"value":"Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-dihydroorotate + NAD(+) = orotate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13513"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30839"},{"database":"ChEBI","id":"CHEBI:30864"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.3.1.14","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048996"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-dihydroorotate + a quinone = orotate + a quinol","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30187"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:30839"},{"database":"ChEBI","id":"CHEBI:30864"},{"database":"ChEBI","id":"CHEBI:132124"}],"ecNumber":"1.3.5.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048639"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Binds 1 FMN per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004715"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005161"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011669"}],"value":"Heterotetramer of 2 PyrK and 2 PyrD type B subunits"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Peripheral membrane protein","id":"SL-9903"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004370"}],"value":"Membrane","id":"SL-0162"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005359"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"value":"Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"Dihydroorotate dehydrogenase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01180"}]},{"type":"Active site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}]},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":326,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00225"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60403.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60403.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS60403.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110893428.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4WIX4","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_27180","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802377at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004589","properties":[{"key":"GoTerm","value":"F:dihydroorotate dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0106430","properties":[{"key":"GoTerm","value":"F:dihydroorotate dehydrogenase (quinone) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006207","properties":[{"key":"GoTerm","value":"P:'de novo' pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd04738","properties":[{"key":"EntryName","value":"DHOD_2_like"},{"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_00225","properties":[{"key":"EntryName","value":"DHO_dh_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR050074","properties":[{"key":"EntryName","value":"DHO_dehydrogenase"}]},{"database":"InterPro","id":"IPR005719","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_2"}]},{"database":"InterPro","id":"IPR005720","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_cat"}]},{"database":"InterPro","id":"IPR001295","properties":[{"key":"EntryName","value":"Dihydroorotate_DH_CS"}]},{"database":"NCBIfam","id":"NF003645","properties":[{"key":"EntryName","value":"PRK05286.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003652","properties":[{"key":"EntryName","value":"PRK05286.2-5"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01036","properties":[{"key":"EntryName","value":"pyrD_sub2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48109:SF4","properties":[{"key":"EntryName","value":"DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48109","properties":[{"key":"EntryName","value":"DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01180","properties":[{"key":"EntryName","value":"DHO_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51395","properties":[{"key":"EntryName","value":"FMN-linked oxidoreductases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00911","properties":[{"key":"EntryName","value":"DHODEHASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00912","properties":[{"key":"EntryName","value":"DHODEHASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLYKSLAKPLLFKMDPEQAHHLIIGGLSGVGKVRPVPSGLRVMYGVRETPDLAVDMFGCHFPTPVGLAAGLDKNGQAVTGFSSIGFGFMEVGTVTPLAQTGNEQPRLFRLPPDEALVNRMGFNNLGAEAMAGELARLQERRIPVAVNIGKNKTTPNEEAHLDYEKCIQALYNYADLFVVNISSPNTPDLRNLQHGNELKELLAAVMSEMNRQQEKHGGASKSVLVKIAPDVNDQELEYMVSTIAASGVSGIIATNTTISREGLSHQHAKETGGLSGKPLRERSTEIIRQVYRQTEGKLPIIGSGGIFTSEDAYEKIKAGASLVEIYTALIYEGPEVNRRIHAGLRELLRKDGYHHISEAVGAEHR","length":365,"molWeight":39745,"crc64":"A9919E22A5B8843F","md5":"5B8B7D57C47B826ED8EB27997B25E8A4"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":14},"uniParcId":"UPI000D96A921"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX6Q7V7","uniProtkbId":"A0ABX6Q7V7_PAEBA","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58294.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional NAD(P)H-hydrate repair enzyme"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Nicotinamide nucleotide repair protein"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent (S)-NAD(P)H-hydrate dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"4.2.1.136"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent NAD(P)HX dehydratase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"NAD(P)H-hydrate epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"5.1.99.6"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"nnrD"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"nnrE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58294.1"}],"value":"HUB98_19960"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025153"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADHX = (6S)-NADHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32215"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:64075"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000013"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADPHX = (6S)-NADPHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32227"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:64077"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000909"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADHX + ADP = AMP + phosphate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32223"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048238"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADPHX + ADP = AMP + phosphate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32235"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Binds 1 potassium ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009524"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the C-terminal section; belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006001"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the N-terminal section; belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":576,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":493,"modifier":"EXACT"},"end":{"value":497,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":522,"modifier":"EXACT"},"end":{"value":522,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":523,"modifier":"EXACT"},"end":{"value":523,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58294.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58294.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS58294.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110898218.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"KEGG","id":"pbac:HUB98_19960","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0052855","properties":[{"key":"GoTerm","value":"F:ADP-dependent NAD(P)H-hydrate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052856","properties":[{"key":"GoTerm","value":"F:NAD(P)HX epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0110051","properties":[{"key":"GoTerm","value":"P:metabolite repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046496","properties":[{"key":"GoTerm","value":"P:nicotinamide nucleotide metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01171","properties":[{"key":"EntryName","value":"YXKO-related"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10260","properties":[{"key":"EntryName","value":"YjeF N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01965","properties":[{"key":"EntryName","value":"NADHX_dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01966","properties":[{"key":"EntryName","value":"NADHX_epimerase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017953","properties":[{"key":"EntryName","value":"Carbohydrate_kinase_pred_CS"}]},{"database":"InterPro","id":"IPR000631","properties":[{"key":"EntryName","value":"CARKD"}]},{"database":"InterPro","id":"IPR030677","properties":[{"key":"EntryName","value":"Nnr"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR004443","properties":[{"key":"EntryName","value":"YjeF_N_dom"}]},{"database":"InterPro","id":"IPR036652","properties":[{"key":"EntryName","value":"YjeF_N_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00196","properties":[{"key":"EntryName","value":"yjeF_cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00197","properties":[{"key":"EntryName","value":"yjeF_nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592:SF0","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01256","properties":[{"key":"EntryName","value":"Carb_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03853","properties":[{"key":"EntryName","value":"YjeF_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF017184","properties":[{"key":"EntryName","value":"Nnr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64153","properties":[{"key":"EntryName","value":"YjeF N-terminal domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS01050","properties":[{"key":"EntryName","value":"YJEF_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51383","properties":[{"key":"EntryName","value":"YJEF_C_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51385","properties":[{"key":"EntryName","value":"YJEF_N"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFIVTADQMRAVDEYTIRQLGIPAVSLMENAGRAIAEEVIKLCREAQGAGSQGEGDGIPHGNGQGKGDVGGYGWPDHGQRKEAWRAHTGPSDHACYGSDILADPALVMAHPGDQHWYMLIGKGNNGGDGLVAARHLVEAGLGVTLVYADAPEALQGEAAVQRDAAAKLGMPAVVHGCEAVDFSRCTGIVDALLGTGSRGAPRGAYAALIRAANDSGKPVVSADVPSGLDADTGEVYEPCIEARVTVCLALLKRGLVQYPGASAAGRIVVRAIGIPARLAPEHGPSVRLLTDEVLRDALRVDTGRRRAPDGHKGTYGHVLLAAGSMPMSGAGLLSAKAALRAGCGLATWALPAALLPHVIGTVPELMLAAAADGDSGEWNAASAAAVLRLAQSRDVLATGPGLGRFKGDTDWLRRLWQQTDRPLVIDADALNMLADAGPDGPRIWGQRSAATILTPHPGEMGRLLRMSTPEVQRDRIGHAARYAREQGVTLVLKGARTVIATPSGEAYINTTGHAGMATGGAGDVLTGIIAGLLAQGLDAEQAAAFGVYLHGQAAERAALLRGDPSSLMAGDIIDAL","length":576,"molWeight":59473,"crc64":"2167448AD6158322","md5":"E669F8B0502E97FB56C232F13D599EF0"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4},"countByFeatureType":{"Domain":2,"Binding site":13},"uniParcId":"UPI000DA11D26"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX6QCU6","uniProtkbId":"A0ABX6QCU6_PAEBA","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60031.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00072883"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066633"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"6.3.2.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075482"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-A2pm-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00076158"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-diaminopimelate-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00081560"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-tripeptide synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramyl-tripeptide synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"murE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60031.1"}],"value":"HUB98_08175"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00056782"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050251"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004752"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":466,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":464,"modifier":"EXACT"},"end":{"value":464,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":468,"modifier":"EXACT"},"end":{"value":468,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Modified residue","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022618"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60031.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60031.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS60031.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"KEGG","id":"pbac:HUB98_08175","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004326","properties":[{"key":"GoTerm","value":"F:tetrahydrofolylpolyglutamate synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.90.190.20:FF:000006","properties":[{"key":"EntryName","value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR018109","properties":[{"key":"EntryName","value":"Folylpolyglutamate_synth_CS"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01011","properties":[{"key":"EntryName","value":"FOLYLPOLYGLU_SYNT_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLLNQFQSQLTTARLVGDSNIECHNLQTDSRQVQPGDLFICLPGHTVDGHDYAAKAVQAGASALVVERELDLAVPQLIVNDSRFAMAVLSDFFFDSPSRKMKMIGVTGTNGKTTTTYLIEKIMSDYGQKTGLIGTIQMRYDGRTYPMSGTTPEALDLQRSLHDMVQAGTDCCVMEVSSHALEQGRVKGTDFRTAVFTNLTQDHLDYHHSMEEYRGAKGLFFARMGNTYADEASLRKYAVINADDPAAAYFISVTAAEVITYGMGEKADVRASEISITAQGTSFHVDTFAGSADIQLRMVGKFNVYNAMAAISAALVEGVPLEEIKRSLETVPGVDGRVEAVDEGQPYAVIVDYAHTPDGLENVLRTVKEFAEGRVICVFGCGGDRDRTKRPLMGKIAAKYSDFVLVTSDNPRTENPDLILKDIEQGLIEDAVPAERYTLIVDRRLAIHEAIEMASPADVVLIAGKGHETYQIIGTTKTDFDDRIIAKEAIRGKSN","length":495,"molWeight":54148,"crc64":"1BFD7AF468ACA2FC","md5":"9DD2DF45ED4A07C363A5B1C03023333E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":10,"Modified residue":1},"uniParcId":"UPI000DA198D4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX6QDD7","uniProtkbId":"A0ABX6QDD7_PAEBA","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60209.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bifunctional protein GlmU"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"UDP-N-acetylglucosamine pyrophosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.7.7.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"N-acetylglucosamine-1-phosphate uridyltransferase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Glucosamine-1-phosphate N-acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.3.1.157"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60209.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60209.1"}],"value":"HUB98_17270"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005166"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005208"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"Nucleotidyl transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00483"}]},{"type":"Domain","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"Mannose-1-phosphate guanyltransferase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF25087"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":423,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":440,"modifier":"EXACT"},"end":{"value":440,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60209.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS60209.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS60209.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"KEGG","id":"pbac:HUB98_17270","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR056729","properties":[{"key":"EntryName","value":"GMPPB_C"}]},{"database":"InterPro","id":"IPR005835","properties":[{"key":"EntryName","value":"NTP_transferase_dom"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"NF010934","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25087","properties":[{"key":"EntryName","value":"GMPPB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00483","properties":[{"key":"EntryName","value":"NTP_transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLKRMAIVLAAGQGKRMKSKLYKVLHPVCGKPMVGHVLDAALRAGVERSVVVVGHGAEAVQSFLGSRAEYALQAEQLGTGHAVKQVKSLLGNESGSTIVVCGDTPLVTSETLEGLMKLHEENGAAATVLTAELEQPKGYGRVIRGEDGSVQRIVEQKDCTPQEDAVKEINTGTYCFDNAKLFAALEKVTNQNAQGEYYLTDVIGIFKNEGEVVEAYMSDDIAESIGVNDRLALSQAEAYMRERLAVRHMLNGVTIIDPSSTYIGADVTIGADTVLYPGTVLKGTTSIGAACHIGPHADIEDSIIQDGAAIKHSVVSKSEIGPDATVGPFANLRPGTKLGRNVKIGDFVEVKNATIDEGSKVSHLSYIGDAQVGKNVNVGCGAITVNYDGYNKAVTTIEDNAFVGSNVNLIAPITVGKGAYVVAGSTVTHSVPENDLAIARARQENKAGYAEKIRGRAKAKKQNAKPE","length":467,"molWeight":49402,"crc64":"A40CA7047623C1FE","md5":"298A86A74C78B9F8F6B7BE4183B6FC8E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Active site":1,"Binding site":18},"uniParcId":"UPI00142D1D87"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A2V4UQN0","uniProtkbId":"A0A2V4UQN0_PAEBA","entryAudit":{"firstPublicDate":"2018-09-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2018-09-12","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Paenibacillus barcinonensis","taxonId":198119,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58081.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Paenibacillaceae","Paenibacillus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"Malonate-semialdehyde dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"MSA dehydrogenase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"1.2.1.27"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"Methylmalonate semialdehyde dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"MMSA dehydrogenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"MSDH"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"iolA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58081.1"}],"value":"HUB98_18635"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively. Is involved in a myo-inositol catabolic pathway. Bicarbonate, and not CO2, is the end-product of the enzymatic reaction"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methyl-3-oxopropanoate + NAD(+) + CoA + H2O = propanoyl-CoA + hydrogencarbonate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20804"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57392"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57700"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.2.1.27","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-oxopropanoate + NAD(+) + CoA + H2O = hydrogencarbonate + acetyl-CoA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:76615"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:33190"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.2.1.27","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 7/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"Belongs to the aldehyde dehydrogenase family. IolA subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"Aldehyde dehydrogenase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00171"}]},{"type":"Active site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10008"}]},{"type":"Binding site","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01670"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B2OOV1T2L147C","citationType":"submission","authors":["Kim M.","Park Y.-J.","Shin J.-H."],"title":"Complete genome of Paenibacillus barcinonensis KACC11450.","publicationDate":"JUN-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58081.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}],"value":"KACC11450","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QKS58081.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000509327"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP054614","properties":[{"key":"ProteinId","value":"QKS58081.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_110899657.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP054614.1"}]},{"database":"AlphaFoldDB","id":"A0A2V4UQN0","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pbac:HUB98_18635","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"20170at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000509327","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0018478","properties":[{"key":"GoTerm","value":"F:malonate-semialdehyde dehydrogenase (acetylating) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004491","properties":[{"key":"GoTerm","value":"F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019310","properties":[{"key":"GoTerm","value":"P:inositol catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006574","properties":[{"key":"GoTerm","value":"P:L-valine catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006210","properties":[{"key":"GoTerm","value":"P:thymine catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd07085","properties":[{"key":"EntryName","value":"ALDH_F6_MMSDH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.309.10:FF:000002","properties":[{"key":"EntryName","value":"Methylmalonate-semialdehyde dehydrogenase (Acylating)"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.605.10:FF:000003","properties":[{"key":"EntryName","value":"Methylmalonate-semialdehyde dehydrogenase [acylating]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.605.10","properties":[{"key":"EntryName","value":"Aldehyde Dehydrogenase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.309.10","properties":[{"key":"EntryName","value":"Aldehyde Dehydrogenase, Chain A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01670","properties":[{"key":"EntryName","value":"IolA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016161","properties":[{"key":"EntryName","value":"Ald_DH/histidinol_DH"}]},{"database":"InterPro","id":"IPR016163","properties":[{"key":"EntryName","value":"Ald_DH_C"}]},{"database":"InterPro","id":"IPR016160","properties":[{"key":"EntryName","value":"Ald_DH_CS_CYS"}]},{"database":"InterPro","id":"IPR016162","properties":[{"key":"EntryName","value":"Ald_DH_N"}]},{"database":"InterPro","id":"IPR015590","properties":[{"key":"EntryName","value":"Aldehyde_DH_dom"}]},{"database":"InterPro","id":"IPR010061","properties":[{"key":"EntryName","value":"MeMal-semiAld_DH"}]},{"database":"InterPro","id":"IPR023510","properties":[{"key":"EntryName","value":"MSDH_GmP_bac"}]},{"database":"NCBIfam","id":"TIGR01722","properties":[{"key":"EntryName","value":"MMSDH"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43866","properties":[{"key":"EntryName","value":"MALONATE-SEMIALDEHYDE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43866:SF4","properties":[{"key":"EntryName","value":"MALONATE-SEMIALDEHYDE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00171","properties":[{"key":"EntryName","value":"Aldedh"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53720","properties":[{"key":"EntryName","value":"ALDH-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00070","properties":[{"key":"EntryName","value":"ALDEHYDE_DEHYDR_CYS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGKGTSEVSAAVTNVQNWIGGAWVTPSTTRTEPVVNPATEEIIAYVPLSEQADVDLAVQTAREAFKSWSGTPVPRRARILFRYQQLLVEHWEELARLVTLENGKSYAEAYGEVLRGIECVEFAAGAPNLMMGKQLPDIATGLESGMFRYPIGVIGGITPFNFPMMVPCWMFPLAIACGNTFVLKPSERTPLLAGRLAELFKEAGLPDGVLNIVHGAHDVVNGLLEHKEVAAISFVGSQPVAEYVYKTASANGKRVQALAGAKNHSIVMPDADLDLTVKEITSAAFGSAGERCMACSVVVAVGDVADTLVQKLVEAADRINIGNGMDEGVFLGPVIRGPHKERTLGYIESGEQEGAALIRDGRKDQATDGSGYFVGPTVFDHVDSTMKIWKDEIFAPVLSVARVETLEEAVELANRSDFANGACLFTRSGANMRQFRETIEAGMLGVNLGVPAPMAFFPFSGWKKSFYGDLHANGTDGVEFYTRKKMVTTRW","length":491,"molWeight":53087,"crc64":"320DAFE819CA6405","md5":"75FE6328D9A31A9384DFB75EBD2AAB86"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":5},"uniParcId":"UPI000D904B78"}}]}