ID BIOB_SALRD Reviewed; 359 AA. AC Q2S4I8; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 107. 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=SRU_0756; OS Salinibacter ruber (strain DSM 13855 / M31). OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae; OC Salinibacter. OX NCBI_TaxID=309807; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13855 / CECT 5946 / M31; RX PubMed=16330755; DOI=10.1073/pnas.0509073102; RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., RA Legault B., Rodriguez-Valera F.; RT "The genome of Salinibacter ruber: convergence and gene exchange among RT hyperhalophilic bacteria and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005). 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; CP000159; ABC44565.1; -; Genomic_DNA. DR RefSeq; WP_011403522.1; NC_007677.1. DR RefSeq; YP_444893.1; NC_007677.1. DR AlphaFoldDB; Q2S4I8; -. DR SMR; Q2S4I8; -. DR STRING; 309807.SRU_0756; -. DR EnsemblBacteria; ABC44565; ABC44565; SRU_0756. DR KEGG; sru:SRU_0756; -. DR PATRIC; fig|309807.25.peg.778; -. DR eggNOG; COG0502; Bacteria. DR HOGENOM; CLU_033172_2_1_10; -. DR OrthoDB; 9786826at2; -. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000008674; 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; 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; 4Fe-4S; Biotin biosynthesis; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..359 FT /note="Biotin synthase" FT /id="PRO_0000381607" FT DOMAIN 47..276 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT REGION 320..359 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 69 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 72 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 109 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 141 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 201 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 271 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" SQ SEQUENCE 359 AA; 39005 MW; 86AE7458EC716DB6 CRC64; MTAWRTLATQ VLNGTPLSSS QALDVVHADD DEVLALLDAA FRVRRHHHGR RVRIHVLQNA KSGVCPEDCA FCSQSLKFDS DPEQYGMQQV DQIVEGAKAA WDKGAVTYCI VTATRGPHSS EVDVVCEATR RIKETYPMDV CASLGLLDAK QARKLADAGV DRYNHNLETS CDHFGNVVTT HEWSDRVETV KQAKAAGMEA CCGGIIGLGE ARADWVDLAL ALREIGVESV PVNFLNPRSG TPLEDVDTVR PQDCLKALAM FRLVHPEADL RMAGGREVVL DQMQPLALYA ANSFFTDGYL TTGGQGESKD YRMIQQAGFE PVIVEDGPER QTPATADDTP SGDPEAADRR RQPSAGPAG //