{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O34539","secondaryAccessions":["Q796N7"],"uniProtkbId":"NDPGT_BACSU","entryAudit":{"firstPublicDate":"2009-01-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1998-01-01","entryVersion":132,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Bacillus subtilis (strain 168)","taxonId":224308,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Bacillaceae","Bacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"NDP-glycosyltransferase YjiC"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28315700"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"value":"2.4.1.384"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"33310191"}],"value":"UDP-glycosyltransferase YjiC"}}]},"genes":[{"geneName":{"value":"yjiC"},"orderedLocusNames":[{"value":"BSU12220"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28315700"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28315700"}],"value":"Glycosyltransferase that can glycosylate a wide range of substrates, including various flavonoids, phenyl ketones, curcuminoid, lignins, zingerone, triterpenes, stilbene and anthraquinone, using UDP-glucose or ADP-glucose as sugar donor (PubMed:28315700, PubMed:33152360). It also exhibits O-, N- and S-glycosylation activities towards simple aromatics (PubMed:28315700). In vivo, the broad acceptor tolerance of YjiC might function as a detoxification agent against exogenous xenobiotics to make the strain adaptable to the changeable environment (Probable)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an NDP-glycose + an acceptor = a glycosylated acceptor + NDP.","ecNumber":"2.4.1.384","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28315700"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28315700"}],"value":"Activity is improved in the presence of Mn(2+), Mg(2+) and Ca(2+), and inhibited by Ni(2+), Zn(2+) and Cu(2+)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":19.4,"unit":"uM","substrate":"apigenin","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28315700"}]},{"constant":22.6,"unit":"uM","substrate":"genistein","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28315700"}]},{"constant":6.795,"unit":"uM","substrate":"2-chloro-4-nitrophenyl glycoside","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28315700"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"value":"kcat is 1.9 sec(-1) with apigenin as substrate. kcat is 1.6 sec(-1) with genistein as substrate (PubMed:28315700). kcat is 164 min(-1) with 2-chloro-4-nitrophenyl glycoside as substrate (PubMed:33152360)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28315700"}],"value":"Optimum pH is approximately 8.0."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28315700"}],"value":"Optimum temperature is 30-40 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33310191"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33310191"}],"value":"Adopts the classical GT-B fold containing the N-terminal and C-terminal domains that accommodate the sugar acceptor and UDP-glucose, respectively (PubMed:33152360, PubMed:33310191). The spacious sugar-acceptor binding pocket might be responsible for the broad substrate spectrum (PubMed:33310191)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the UDP-glycosyltransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"NDP-glycosyltransferase YjiC","featureId":"PRO_0000360169"},{"type":"Binding site","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58223"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33310191"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6KQX"}],"ligand":{"name":"UDP","id":"ChEBI:CHEBI:58223"}},{"type":"Binding site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58223"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33310191"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6KQX"}],"ligand":{"name":"UDP","id":"ChEBI:CHEBI:58223"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58223"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33310191"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6KQX"}],"ligand":{"name":"UDP","id":"ChEBI:CHEBI:58223"}},{"type":"Binding site","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58223"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33310191"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6KQX"}],"ligand":{"name":"UDP","id":"ChEBI:CHEBI:58223"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58223"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33310191"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6KQX"}],"ligand":{"name":"UDP","id":"ChEBI:CHEBI:58223"}},{"type":"Binding site","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58223"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33310191"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6KQX"}],"ligand":{"name":"UDP","id":"ChEBI:CHEBI:58223"}},{"type":"Mutagenesis","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"Drastic loss of activity for both pterostilbene glycosylation and UDP glycosylation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Significant decrease in activity for both pterostilbene glycosylation and UDP glycosylation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"Shows slightly reduced activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"Increases pterostilbene glycosylation activity and UDP glycosylation efficiency.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"V","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"No change in activity. Dramatic reduction of the catalytic efficiency and glycosylation levels; when associated with A-129.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"No change in activity. Dramatic reduction of the catalytic efficiency and glycosylation levels; when associated with A-128.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"Significant reduction in catalytic efficiency and glycosylation levels.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"Strong decrease in activity for both pterostilbene glycosylation and UDP glycosylation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"Significantly enhances the UDP glycosylation efficiency, but shows unchanged or reduced pterostilbene glycosylation when supplied with UDP-glucose and ADP-glucose, respectively.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["F"]}},{"type":"Mutagenesis","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"Enhances the catalytic efficiency of UDP glycosylation, but reduces the relative activity of pterostilbene glycosylation reaction.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["W"]}},{"type":"Mutagenesis","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"Strong decrease in activity for both pterostilbene glycosylation and UDP glycosylation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"Strong decrease in activity for both pterostilbene glycosylation and UDP glycosylation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"Significant reduction in catalytic efficiency and glycosylation levels.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"M","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Almost abolishes the glycosyltransferase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Strong decrease in activity for both pterostilbene glycosylation and UDP glycosylation.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["D"]}},{"type":"Mutagenesis","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"Leads to about 2-fold decrease in specific activities.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"Q","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"Increases UDP glycosylation efficiency and enhances pterostilbene glycosylation activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33152360"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["A"]}},{"type":"Beta strand","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Turn","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQX"}]},{"type":"Beta strand","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7BOV"}]},{"type":"Turn","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"7BOV"}]},{"type":"Beta strand","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQX"}]},{"type":"Helix","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQX"}]},{"type":"Helix","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQX"}]},{"type":"Beta strand","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Beta strand","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]},{"type":"Helix","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6KQW"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"9579062","citationType":"journal article","authors":["Rivolta C.","Soldo B.","Lazarevic V.","Joris B.","Mauel C.","Karamata D."],"citationCrossReferences":[{"database":"PubMed","id":"9579062"},{"database":"DOI","id":"10.1099/00221287-144-4-877"}],"title":"A 35.7 kb DNA fragment from the Bacillus subtilis chromosome containing a putative 12.3 kb operon involved in hexuronate catabolism and a perfectly symmetrical hypothetical catabolite-responsive element.","publicationDate":"1998","journal":"Microbiology","firstPage":"877","lastPage":"884","volume":"144"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"168","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"9384377","citationType":"journal article","authors":["Kunst F.","Ogasawara N.","Moszer I.","Albertini A.M.","Alloni G.","Azevedo V.","Bertero M.G.","Bessieres P.","Bolotin A.","Borchert S.","Borriss R.","Boursier L.","Brans A.","Braun M.","Brignell S.C.","Bron S.","Brouillet S.","Bruschi C.V.","Caldwell B.","Capuano V.","Carter N.M.","Choi S.-K.","Codani J.-J.","Connerton I.F.","Cummings N.J.","Daniel R.A.","Denizot F.","Devine K.M.","Duesterhoeft A.","Ehrlich S.D.","Emmerson P.T.","Entian K.-D.","Errington J.","Fabret C.","Ferrari E.","Foulger D.","Fritz C.","Fujita M.","Fujita Y.","Fuma S.","Galizzi A.","Galleron N.","Ghim S.-Y.","Glaser P.","Goffeau A.","Golightly E.J.","Grandi G.","Guiseppi G.","Guy B.J.","Haga K.","Haiech J.","Harwood C.R.","Henaut A.","Hilbert H.","Holsappel S.","Hosono S.","Hullo M.-F.","Itaya M.","Jones L.-M.","Joris B.","Karamata D.","Kasahara Y.","Klaerr-Blanchard M.","Klein C.","Kobayashi Y.","Koetter P.","Koningstein G.","Krogh S.","Kumano M.","Kurita K.","Lapidus A.","Lardinois S.","Lauber J.","Lazarevic V.","Lee S.-M.","Levine A.","Liu H.","Masuda S.","Mauel C.","Medigue C.","Medina N.","Mellado R.P.","Mizuno M.","Moestl D.","Nakai S.","Noback M.","Noone D.","O'Reilly M.","Ogawa K.","Ogiwara A.","Oudega B.","Park S.-H.","Parro V.","Pohl T.M.","Portetelle D.","Porwollik S.","Prescott A.M.","Presecan E.","Pujic P.","Purnelle B.","Rapoport G.","Rey M.","Reynolds S.","Rieger M.","Rivolta C.","Rocha E.","Roche B.","Rose M.","Sadaie Y.","Sato T.","Scanlan E.","Schleich S.","Schroeter R.","Scoffone F.","Sekiguchi J.","Sekowska A.","Seror S.J.","Serror P.","Shin B.-S.","Soldo B.","Sorokin A.","Tacconi E.","Takagi T.","Takahashi H.","Takemaru K.","Takeuchi M.","Tamakoshi A.","Tanaka T.","Terpstra P.","Tognoni A.","Tosato V.","Uchiyama S.","Vandenbol M.","Vannier F.","Vassarotti A.","Viari A.","Wambutt R.","Wedler E.","Wedler H.","Weitzenegger T.","Winters P.","Wipat A.","Yamamoto H.","Yamane K.","Yasumoto K.","Yata K.","Yoshida K.","Yoshikawa H.-F.","Zumstein E.","Yoshikawa H.","Danchin A."],"citationCrossReferences":[{"database":"PubMed","id":"9384377"},{"database":"DOI","id":"10.1038/36786"}],"title":"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.","publicationDate":"1997","journal":"Nature","firstPage":"249","lastPage":"256","volume":"390"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"168","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"28315700","citationType":"journal article","authors":["Dai L.","Li J.","Yao P.","Zhu Y.","Men Y.","Zeng Y.","Yang J.","Sun Y."],"citationCrossReferences":[{"database":"PubMed","id":"28315700"},{"database":"DOI","id":"10.1016/j.jbiotec.2017.03.009"}],"title":"Exploiting the aglycon promiscuity of glycosyltransferase Bs-YjiC from Bacillus subtilis and its application in synthesis of glycosides.","publicationDate":"2017","journal":"J. Biotechnol.","firstPage":"69","lastPage":"76","volume":"248"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES"],"referenceComments":[{"value":"168","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"33310191","citationType":"journal article","authors":["Dai L.","Qin L.","Hu Y.","Huang J.W.","Hu Z.","Min J.","Sun Y.","Guo R.T."],"citationCrossReferences":[{"database":"PubMed","id":"33310191"},{"database":"DOI","id":"10.1016/j.bbrc.2020.11.104"}],"title":"Structural dissection of unnatural ginsenoside-biosynthetic UDP-glycosyltransferase Bs-YjiC from Bacillus subtilis for substrate promiscuity.","publicationDate":"2021","journal":"Biochem. Biophys. Res. Commun.","firstPage":"73","lastPage":"78","volume":"534"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 1-387 IN COMPLEX WITH UDP","SUBUNIT","DOMAIN"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"6KQW"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"6KQX"}]},{"referenceNumber":5,"citation":{"id":"33152360","citationType":"journal article","authors":["Liu B.","Zhao C.","Xiang Q.","Zhao N.","Luo Y.","Bao R."],"citationCrossReferences":[{"database":"PubMed","id":"33152360"},{"database":"DOI","id":"10.1016/j.ijbiomac.2020.10.238"}],"title":"Structural and biochemical studies of the glycosyltransferase Bs-YjiC from Bacillus subtilis.","publicationDate":"2021","journal":"Int. J. Biol. Macromol.","firstPage":"806","lastPage":"817","volume":"166"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS)","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","DOMAIN","MUTAGENESIS OF HIS-16; ASP-106; PHE-107; VAL-108; SER-128; SER-129; TYR-130; THR-229; SER-277; HIS-293; GLU-301; MET-315; GLU-317; GLN-318 AND LEU-320"],"referenceComments":[{"value":"168","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"7BOV"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF015825","properties":[{"key":"ProteinId","value":"AAC46318.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AL009126","properties":[{"key":"ProteinId","value":"CAB13079.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"C69851","properties":[{"key":"EntryName","value":"C69851"}]},{"database":"RefSeq","id":"WP_003232783.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000964.3"}]},{"database":"PDB","id":"6KQW","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.18 A"},{"key":"Chains","value":"A=1-387"}]},{"database":"PDB","id":"6KQX","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.44 A"},{"key":"Chains","value":"A=1-392"}]},{"database":"PDB","id":"7BOV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.29 A"},{"key":"Chains","value":"A=1-392"}]},{"database":"PDBsum","id":"6KQW","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"6KQX","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"7BOV","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"O34539","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O34539","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"O34539","properties":[{"key":"Number of interactors","value":"28"}]},{"database":"STRING","id":"224308.BSU12220","properties":[{"key":"Description","value":"-"}]},{"database":"jPOST","id":"O34539","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"224308-BSU12220","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"CAB13079","properties":[{"key":"ProteinId","value":"CAB13079"},{"key":"GeneId","value":"BSU_12220"}]},{"database":"GeneID","id":"939402","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"bsu:BSU12220","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|224308.179.peg.1320","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG1819","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"InParanoid","id":"O34539","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"6620093at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"O34539","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"BSUB:BSU12220-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.4.1.384","properties":[{"key":"OrganismId","value":"658"}]},{"database":"Proteomes","id":"UP000001570","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"AbasyAtlas","id":"O34539","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0016758","properties":[{"key":"GoTerm","value":"F:hexosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008194","properties":[{"key":"GoTerm","value":"F:UDP-glycosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0017000","properties":[{"key":"GoTerm","value":"P:antibiotic biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd03784","properties":[{"key":"EntryName","value":"GT1_Gtf-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2000:FF:000072","properties":[{"key":"EntryName","value":"Glycosyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2000","properties":[{"key":"EntryName","value":"Glycogen Phosphorylase B"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR010610","properties":[{"key":"EntryName","value":"EryCIII-like_C"}]},{"database":"InterPro","id":"IPR050426","properties":[{"key":"EntryName","value":"Glycosyltransferase_28"}]},{"database":"InterPro","id":"IPR002213","properties":[{"key":"EntryName","value":"UDP_glucos_trans"}]},{"database":"InterPro","id":"IPR006326","properties":[{"key":"EntryName","value":"UDPGT_MGT-like"}]},{"database":"NCBIfam","id":"TIGR01426","properties":[{"key":"EntryName","value":"MGT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48050","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48050:SF13","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE UGT80A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06722","properties":[{"key":"EntryName","value":"EryCIII-like_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53756","properties":[{"key":"EntryName","value":"UDP-Glycosyltransferase/glycogen phosphorylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKYHISMINIPAYGHVNPTLALVEKLCEKGHRVTYATTEEFAPAVQQAGGEALIYHTSLNIDPKQIREMMEKNDAPLSLLKESLSILPQLEELYKDDQPDLIIYDFVALAGKLFAEKLNVPVIKLCSSYAQNESFQLGNEDMLKKIREAEAEFKAYLEQEKLPAVSFEQLAVPEALNIVFMPKSFQIQHETFDDRFCFVGPSLGERKEKESLLIDKDDRPLMLISLGTAFNAWPEFYKMCIKAFRDSSWQVIMSVGKTIDPESLEDIPANFTIRQSVPQLEVLEKADLFISHGGMNSTMEAMNAGVPLVVIPQMYEQELTANRVDELGLGVYLPKEEVTVSSLQEAVQAVSSDQELLSRVKNMQKDVKEAGGAERAAAEIEAFMKKSAVPQ","length":392,"molWeight":43988,"crc64":"3830835750C5E896","md5":"CFAA153FA3288F0A5AA2D99F92DC5A0F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":6,"Mutagenesis":17,"Beta strand":16,"Helix":17,"Turn":2},"uniParcId":"UPI0000060256"}}