ID BIOB_GEOKA Reviewed; 333 AA. AC Q5KZN1; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, 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}; OrderedLocusNames=GK1570; OS Geobacillus kaustophilus (strain HTA426). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus; OC Geobacillus thermoleovorans group. OX NCBI_TaxID=235909; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTA426; RX PubMed=15576355; DOI=10.1093/nar/gkh970; RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., RA Matsui S., Uchiyama I.; RT "Thermoadaptation trait revealed by the genome sequence of thermophilic RT Geobacillus kaustophilus."; RL Nucleic Acids Res. 32:6292-6303(2004). 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; BA000043; BAD75855.1; -; Genomic_DNA. DR RefSeq; WP_011231066.1; NC_006510.1. DR AlphaFoldDB; Q5KZN1; -. DR SMR; Q5KZN1; -. DR STRING; 235909.GK1570; -. DR KEGG; gka:GK1570; -. DR eggNOG; COG0502; Bacteria. DR HOGENOM; CLU_033172_2_1_9; -. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000001172; 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..333 FT /note="Biotin synthase" FT /id="PRO_0000381401" FT DOMAIN 47..273 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" 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 333 AA; 36518 MW; C025951F519D9E1B CRC64; MANWLVLAEQ VLGGHELTDE EALAILDCPD EELLLLLQGA YRIRSAYYGN KVKLNMIINA KSGLCPENCG YCSQSAVSTA PVKTYKMVDK ETLLRGAEEA HRLRIGTYCI VASGRGPSDK EIDTVVSAVK EIKERFGLKV CACLGILKPE QAARLKEAGV DRYNHNINTS KQHHPNITTS HTYDDRVRTV ETVKEAGLSP CSGVIIGMKE TKRDVVDMAR SLRALDADSI PVNFLHAIDG TPLAGTNELN PRYCLKVLAL FRYMNPTKEI RIAGGREVNL RSLQPLGLYA ANSIFVGDYL TTAGQEKSAD YQMLEDLGFE IEFAPAPQAG VVS //