ID A0A154BLZ1_ANASB Unreviewed; 330 AA. AC A0A154BLZ1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 24-JUL-2024, entry version 35. DE RecName: Full=Biotin synthase {ECO:0000256|ARBA:ARBA00012236, ECO:0000256|HAMAP-Rule:MF_01694}; DE EC=2.8.1.6 {ECO:0000256|ARBA:ARBA00012236, ECO:0000256|HAMAP-Rule:MF_01694}; GN Name=bioB {ECO:0000256|HAMAP-Rule:MF_01694}; GN ORFNames=AXX12_15260 {ECO:0000313|EMBL:KYZ74936.1}; OS Anaerosporomusa subterranea. OC Bacteria; Bacillota; 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 obligate RT anaerobe isolated from saprolite."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_01694}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe- CC 2S]-[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:59789, ChEBI:CHEBI:64428, ChEBI:CHEBI:149473; EC=2.8.1.6; CC Evidence={ECO:0000256|ARBA:ARBA00023417, ECO:0000256|HAMAP- CC Rule:MF_01694}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01694}; CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 CC cysteines and 1 arginine. {ECO:0000256|HAMAP-Rule:MF_01694}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000256|PIRSR:PIRSR001619-1}; CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 CC cysteines and 1 arginine. {ECO:0000256|PIRSR:PIRSR001619-1}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01694, CC ECO:0000256|PIRSR:PIRSR001619-1}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|PIRSR:PIRSR001619-1}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8- CC diaminononanoate: step 2/2. {ECO:0000256|ARBA:ARBA00004942, CC ECO:0000256|HAMAP-Rule:MF_01694}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01694}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase CC family. {ECO:0000256|ARBA:ARBA00010765, ECO:0000256|HAMAP- CC Rule:MF_01694}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A154BLZ1; -. DR STRING; 1794912.AXX12_15260; -. DR OrthoDB; 9786826at2; -. 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-UniRule. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01335; Radical_SAM; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 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/MiaA/NifB-like_rSAM. DR InterPro; IPR007197; rSAM. DR NCBIfam; TIGR00433; bioB; 1. DR PANTHER; PTHR22976; BIOTIN SYNTHASE; 1. DR PANTHER; PTHR22976:SF2; BIOTIN SYNTHASE, MITOCHONDRIAL; 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 SFLD; SFLDS00029; Radical_SAM; 1. DR SMART; SM00876; BATS; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. PE 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_01694}; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01694}; KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756, ECO:0000256|HAMAP- KW Rule:MF_01694}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01694}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_01694}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01694}; Reference proteome {ECO:0000313|Proteomes:UP000076268}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_01694}; Transferase {ECO:0000256|HAMAP-Rule:MF_01694}. FT DOMAIN 49..280 FT /note="Radical SAM core" FT /evidence="ECO:0000259|PROSITE:PS51918" FT BINDING 67 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT BINDING 71 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT BINDING 74 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT BINDING 112 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT BINDING 145 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT BINDING 205 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT BINDING 275 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="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 //