ID BIOB_AKKM8 Reviewed; 321 AA. AC B2UNW0; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 23-FEB-2022, entry version 75. 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=Amuc_0492; OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC OS 81048 / CCUG 64013 / CIP 107961 / Muc). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Akkermansiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP RC 107961 / Muc; RX PubMed=21390229; DOI=10.1371/journal.pone.0016876; RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M., RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.; RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin RT degrader, and its use in exploring intestinal metagenomes."; RL PLoS ONE 6:E16876-E16876(2011). 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:49601; 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; CP001071; ACD04330.1; -; Genomic_DNA. DR RefSeq; WP_012419545.1; NC_010655.1. DR SMR; B2UNW0; -. DR STRING; 349741.Amuc_0492; -. DR EnsemblBacteria; ACD04330; ACD04330; Amuc_0492. DR KEGG; amu:Amuc_0492; -. DR eggNOG; COG0502; Bacteria. DR HOGENOM; CLU_033172_2_1_0; -. DR OMA; AMGVHRY; -. DR OrthoDB; 940969at2; -. DR BioCyc; AMUC349741:G1GBX-541-MONOMER; -. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000001031; 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 Gene3D; 3.20.20.70; -; 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/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR PANTHER; PTHR22976; PTHR22976; 1. DR Pfam; PF06968; BATS; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF001619; Biotin_synth; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SMART; SM00876; BATS; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00433; bioB; 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..321 FT /note="Biotin synthase" FT /id="PRO_0000381189" FT DOMAIN 44..273 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT METAL 62 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT METAL 66 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT METAL 69 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT METAL 106 FT /note="Iron-sulfur (2Fe-2S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT METAL 138 FT /note="Iron-sulfur (2Fe-2S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT METAL 198 FT /note="Iron-sulfur (2Fe-2S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT METAL 268 FT /note="Iron-sulfur (2Fe-2S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" SQ SEQUENCE 321 AA; 35189 MW; CB8D64273798981E CRC64; MSLTSSLLSR VLGGGSCSRE ELIALSREPL EELCQAANAI REHFCGNVFD LCTIINGRSG KCSENCKYCA QSAHYSTAVE EYPLLSDEAL LAGARYNDAR GILRYSIVTS GKRLTDEDVD RLCASYRHIA EHCGISLCAS HGLISKKHCE QLKAAGVSRY HNNLETSRRN FPNVCTTHTY DDKLQTIKWA LEAGLEVCSG GIMGLGETME DRIDMYMDIA ALGIKSMPVN FLTPIPGTPY ADMTPLGEEE QLRIVALVRF IMPDGFVRIA AGRNTMKDHG RKIFMSGANA AISGDMLTTA GVTIREDLAM LAELGYEVRM K //