ID   BIOB_RUTMC              Reviewed;         322 AA.
AC   A1AWE7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-SEP-2015, entry version 62.
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};
GN   OrderedLocusNames=Rmag_0499;
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria;
OC   sulfur-oxidizing symbionts; Candidatus Ruthia.
OX   NCBI_TaxID=413404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A.,
RA   Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(2007).
CC   -!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin
CC       by the insertion of a sulfur atom into dethiobiotin via a radical-
CC       based mechanism. {ECO:0000255|HAMAP-Rule:MF_01694}.
CC   -!- CATALYTIC ACTIVITY: Dethiobiotin + sulfur-(sulfur carrier) + 2 S-
CC       adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin +
CC       (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2
CC       oxidized [2Fe-2S] ferredoxin. {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
CC       7,8-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
CC       synthase family. {ECO:0000255|HAMAP-Rule:MF_01694}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000488; ABL02254.1; -; Genomic_DNA.
DR   RefSeq; WP_011737879.1; NC_008610.1.
DR   ProteinModelPortal; A1AWE7; -.
DR   STRING; 413404.Rmag_0499; -.
DR   EnsemblBacteria; ABL02254; ABL02254; Rmag_0499.
DR   KEGG; rma:Rmag_0499; -.
DR   PATRIC; 32000675; VBICanRut45856_0556.
DR   eggNOG; COG0502; -.
DR   HOGENOM; HOG000239957; -.
DR   KO; K01012; -.
DR   OMA; ADRFCMG; -.
DR   OrthoDB; EOG622PMP; -.
DR   BioCyc; CRUT413404:GHM7-519-MONOMER; -.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000002587; 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-HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP.
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   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;
KW   2Fe-2S; 4Fe-4S; Biotin biosynthesis; Complete proteome; Iron;
KW   Iron-sulfur; Metal-binding; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    322       Biotin synthase.
FT                                /FTId=PRO_0000381591.
FT   METAL        54     54       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL        58     58       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL        61     61       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL        98     98       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL       129    129       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL       189    189       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL       261    261       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
SQ   SEQUENCE   322 AA;  36131 MW;  1C8E95F361741BC0 CRC64;
     MEELRNDWTL KEVEILFSLP FNDLLFQAHR IHRQNFDPNQ IQVSSLLNIK TGACPEDCSY
     CSQSSKYDTG LEREKLMEID LVLQQAKEAQ DIGATRFCMG AAWRNPTDKS LAKVILMIQG
     VKTMGMETCV TLGMLTQEQA FILKEAGLDY YNHNIDTSKE HYSNVVTTRN FQDRLNTLES
     VQNANIHVCS GGILGLDESQ TDRASMLRSL SNLRTHPDSV PFNLLVPIPG TPFENIEPPT
     ESEFVRTIAV ARIMMPKSVV RLSAGRTKMG EAMQALCFFA GANSIFYGEQ LLTTDNPNIN
     SDKDLFARLG INQKKVNNLQ SV
//