(data stored in ACNUC9435 zone)

SWISSPROT: BIOB_CLOD6

ID   BIOB_CLOD6              Reviewed;         325 AA.
AC   Q18D35;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   11-DEC-2019, entry version 82.
DE   RecName: Full=Biotin synthase {ECO:0000255|HAMAP-Rule:MF_01694};
DE            EC=2.8.1.6 {ECO:0000255|HAMAP-Rule:MF_01694};
GN   Name=bioB {ECO:0000255|HAMAP-Rule:MF_01694}; OrderedLocusNames=CD630_02970;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
CC   -!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin by
CC       the insertion of a sulfur atom into dethiobiotin via a radical-based
CC       mechanism. {ECO:0000255|HAMAP-Rule:MF_01694}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-SH + dethiobiotin + 2 reduced [2Fe-2S]-
CC         [ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine +
CC         [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-
CC         [ferredoxin]; Xref=Rhea:RHEA:22060, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:29917, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57586, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:57861, ChEBI:CHEBI:59789, ChEBI:CHEBI:64428; EC=2.8.1.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01694};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01694};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_01694};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01694};
CC       Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3
CC       cysteines and 1 arginine. {ECO:0000255|HAMAP-Rule:MF_01694};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC       diaminononanoate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01694}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01694}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01694}.
DR   EMBL; AM180355; CAJ67119.1; -; Genomic_DNA.
DR   RefSeq; WP_009895370.1; NZ_CP010905.2.
DR   RefSeq; YP_001086766.1; NC_009089.1.
DR   SMR; Q18D35; -.
DR   STRING; 272563.CD630_02970; -.
DR   EnsemblBacteria; CAJ67119; CAJ67119; CD630_02970.
DR   GeneID; 4913622; -.
DR   KEGG; cdf:CD630_02970; -.
DR   KEGG; pdc:CDIF630_00422; -.
DR   PATRIC; fig|272563.120.peg.316; -.
DR   eggNOG; ENOG4105CZF; Bacteria.
DR   eggNOG; COG0502; LUCA.
DR   HOGENOM; HOG000239958; -.
DR   KO; K01012; -.
DR   OMA; AMGVHRY; -.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01694; BioB; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR010722; BATS_dom.
DR   InterPro; IPR002684; Biotin_synth/BioAB.
DR   InterPro; IPR024177; Biotin_synthase.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR22976; PTHR22976; 1.
DR   Pfam; PF06968; BATS; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF001619; Biotin_synth; 1.
DR   SMART; SM00876; BATS; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00433; bioB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q18D35.
DR   SWISS-2DPAGE; Q18D35.
KW   2Fe-2S; 4Fe-4S; Biotin biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..325
FT                   /note="Biotin synthase"
FT                   /id="PRO_0000381317"
FT   METAL           69
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           73
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           76
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           113
FT                   /note="Iron-sulfur 2 (2Fe-2S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           145
FT                   /note="Iron-sulfur 2 (2Fe-2S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           205
FT                   /note="Iron-sulfur 2 (2Fe-2S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           275
FT                   /note="Iron-sulfur 2 (2Fe-2S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
SQ   SEQUENCE   325 AA;  36875 MW;  7EE59E789B0267F1 CRC64;
     MEKYIIKLKN KVLREKEISY EEALNLISLD TNNKNDFDIL LKSANEIREY FMGRKADLCT
     IMNAKSGKCS EDCKFCAQSS YYKTGVEEYS LLDYNEILNR AKEMESKGVH RFSLVTSGKG
     MSGKEFNNIL NIYEGLRENT NLKLCASLGI IDYEQAKMLK SAGVTTYHHN VETCRDNFHN
     ICTTHTYKDR IKTIKDAKKA GLDVCVGGII GMNESEEQRL KMAFEIRELN VKSFPINILN
     PIKNTPMENY DVLEPMEILK TTAVFRFIIP NVYIRYAGGR LSLKGYDKVG FNGGVNSAIV
     GDYLTTVGSG IENDKKMIIE QGFEL
//

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