ID BIOB_SHEB8 Reviewed; 350 AA. AC A6WM55; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 87. 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=Shew185_1751; OS Shewanella baltica (strain OS185). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=402882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS185; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.; RT "Complete sequence of chromosome of Shewanella baltica OS185."; RL Submitted (JUL-2007) 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:0000255|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: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:190135; 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}. 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; CP000753; ABS07894.1; -; Genomic_DNA. DR RefSeq; WP_006081265.1; NC_009665.1. DR AlphaFoldDB; A6WM55; -. DR SMR; A6WM55; -. DR GeneID; 11772018; -. DR KEGG; sbm:Shew185_1751; -. DR HOGENOM; CLU_033172_1_2_6; -. DR UniPathway; UPA00078; UER00162. 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; SFLDF00272; biotin_synthase; 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; 4Fe-4S; Biotin biosynthesis; Iron; Iron-sulfur; Metal-binding; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..350 FT /note="Biotin synthase" FT /id="PRO_0000381615" FT DOMAIN 41..268 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 56 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 60 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 63 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 100 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 131 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 191 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 263 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" SQ SEQUENCE 350 AA; 38783 MW; 9B6A317D5553E1AC CRC64; MSQLQVRHDW KREEIEALFA LPMNDLLFKA HSIHREVYDP NEVQISRLLS IKTGACPEDC KYCPQSARYD TGLEKERLLA METVLTEARS AKAAGASRFC MGAAWRNPKE KDMPYLKQMV QEVKALGMET CMTLGMLSED QANDLASAGL DYYNHNLDTS PEYYGDVITT RTYQNRLDTL TNVRASGMKV CSGGIVGMGE KATDRAGLLQ QLANLPQHPD SVPINMLVKV AGTPFEKLDD LDPLEFVRTI AVARILMPLS RVRLSAGREN MSDELQAMCF FAGANSIFYG CKLLTTPNPE ESDDMGLFRR LGLRPEQGAA AKLEEESAVL AKAAAYQDKS SAQFYDAGAL //