ID BIOB_STACT Reviewed; 336 AA. AC B9DKN5; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 86. 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=Sca_2002; OS Staphylococcus carnosus (strain TM300). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=396513; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM300; RX PubMed=19060169; DOI=10.1128/aem.01982-08; RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C., RA Goetz F.; RT "Genome analysis of the meat starter culture bacterium Staphylococcus RT carnosus TM300."; RL Appl. Environ. Microbiol. 75:811-822(2009). 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; AM295250; CAL28907.1; -; Genomic_DNA. DR RefSeq; WP_015901243.1; NC_012121.1. DR AlphaFoldDB; B9DKN5; -. DR SMR; B9DKN5; -. DR GeneID; 60544286; -. DR KEGG; sca:SCA_2002; -. DR eggNOG; COG0502; Bacteria. DR HOGENOM; CLU_033172_2_1_9; -. DR OrthoDB; 9786826at2; -. DR BioCyc; SCAR396513:SCA_RS10135-MONOMER; -. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000000444; 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 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; SFLDG01060; BATS_domain_containing; 1. DR SFLD; SFLDG01278; biotin_synthase_like; 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..336 FT /note="Biotin synthase" FT /id="PRO_0000381656" FT DOMAIN 43..269 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 61 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 65 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 68 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 104 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 137 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 197 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 267 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" SQ SEQUENCE 336 AA; 37506 MW; 554463E9C0BD5458 CRC64; MDTAHKIING YALTKQEAYD LYTDETIDTF TLLDEAYAVR KHYYGKKVKL NMILNAKSGI CPEDCGYCGQ SRDMKRKDRY ALIPENDIIA GANAAADNQI GTYCIVMSGR GPSDKEVDHI TESVRQIKEN HPQLKVCACL GLANEDQASR LKEAGVDRYN HNLNTSENYH DTVVTTHTYE DRVKTVEIMK ENNISPCSGV ICGMGETAQD RIDMAFALKE LDADSIPINF LHPIQGTKFG EMDELTPMKC LRIIAIFRLV NPTKEIRIAG GREVNLQSLQ PFALLAANSI FVGDYLITGG QPNTMDYRMI QDLGFEIDCS NLPEDTAEKI TETLEA //