ID A0A154BLZ1_9FIRM Unreviewed; 330 AA. AC A0A154BLZ1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=Biotin synthase {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|SAAS:SAAS00833216}; DE EC=2.8.1.6 {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|SAAS:SAAS00391055}; GN Name=bioB {ECO:0000256|HAMAP-Rule:MF_01694}; GN ORFNames=AXX12_15260 {ECO:0000313|EMBL:KYZ74936.1}; OS Anaerosporomusa subterranea. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae; OC Anaerosporomusa. OX NCBI_TaxID=1794912 {ECO:0000313|EMBL:KYZ74936.1, ECO:0000313|Proteomes:UP000076268}; RN [1] {ECO:0000313|EMBL:KYZ74936.1, ECO:0000313|Proteomes:UP000076268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RU4 {ECO:0000313|EMBL:KYZ74936.1, RC ECO:0000313|Proteomes:UP000076268}; RA Choi J.K., Shah M., Yee N.; RT "Anaerosporomusa subterraneum gen. nov., sp. nov., a spore-forming RT obligate anaerobe isolated from saprolite."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_01694, CC ECO:0000256|SAAS:SAAS00833214}. 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:0000256|HAMAP-Rule:MF_01694, CC ECO:0000256|SAAS:SAAS00190209}. CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from CC 7,8-diaminononanoate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01694, CC ECO:0000256|SAAS:SAAS00370166}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01694, CC ECO:0000256|SAAS:SAAS00063319}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin CC synthase family. {ECO:0000256|HAMAP-Rule:MF_01694, CC ECO:0000256|SAAS:SAAS00577385}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYZ74936.1}. 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; LSGP01000026; KYZ74936.1; -; Genomic_DNA. DR RefSeq; WP_066245424.1; NZ_LSGP01000026.1. DR EnsemblBacteria; KYZ74936; KYZ74936; AXX12_15260. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000076268; Unassembled WGS sequence. 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 PANTHER; PTHR22976; PTHR22976; 1. DR Pfam; PF06968; BATS; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF001619; Biotin_synth; 1. DR SFLD; SFLDG01278; biotin_synthase_like; 1. DR SMART; SM00876; BATS; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00433; bioB; 1. PE 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|PIRSR:PIRSR001619-1, ECO:0000256|SAAS:SAAS00063334}; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|PIRSR:PIRSR001619-1, ECO:0000256|SAAS:SAAS00063352}; KW Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|SAAS:SAAS00063242}; KW Complete proteome {ECO:0000313|Proteomes:UP000076268}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|PIRSR:PIRSR001619- KW 1, ECO:0000256|SAAS:SAAS00063343}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|PIRSR:PIRSR001619-1, ECO:0000256|SAAS:SAAS00063338}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|PIRSR:PIRSR001619-1, ECO:0000256|SAAS:SAAS00063322}; KW Reference proteome {ECO:0000313|Proteomes:UP000076268}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|PIRSR:PIRSR001619-1, ECO:0000256|SAAS:SAAS00063330}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|SAAS:SAAS00063301}. FT DOMAIN 57 267 Elp3. {ECO:0000259|SMART:SM00729}. FT DOMAIN 235 326 BATS. {ECO:0000259|SMART:SM00876}. FT METAL 67 67 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1}. FT METAL 71 71 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1}. FT METAL 74 74 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1}. FT METAL 112 112 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1}. FT METAL 145 145 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1}. FT METAL 205 205 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1}. FT METAL 275 275 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1}. SQ SEQUENCE 330 AA; 36300 MW; 39110FEC6B4E1B66 CRC64; MSLTFLCEIG NKVLNGGAVT FDEALALTQI KENDIPILLG IANKVRDEFT GKEVDTCEIV NARSGNCSEN CKFCAQSAHH KEVKLTVYSL MSEEEIVAAA KKAEIEGAYR FCIVTAGCGM KSDPDFPKIL SAIERIGRET SLNRCCSLGT LETSHVKELK AAGITRYHHN LETSRSYFQE ICTTHTYDER VQTIKRIKAA GLQACSGCII GMGESWRQRI ELAFELKELD VDSIPINVLN AIEGTALEDQ PRLNPMEILQ TFAIFRLILP TKIIRYAGGR EHNLGELTPL GFLAGINGML MGNYLTTHGR QAADDLKTVR GLGLTPLQSS //