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 19-JAN-2010, entry version 14. DE RecName: Full=Biotin synthase; DE EC=2.8.1.6; DE AltName: Full=Biotin synthetase; GN Name=bioB; OrderedLocusNames=Amuc_0492; OS Akkermansia muciniphila (strain ATCC BAA-835). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., RA de Vos W.M., Richardson P.; RT "Complete sequence of Akkermansia muciniphila ATCC BAA-835."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin CC by the insertion of a sulfur atom into dethiobiotin via a radical- CC based mechanism (By similarity). CC -!- CATALYTIC ACTIVITY: Dethiobiotin + sulfur + 2 S-adenosyl-L- CC methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine. CC -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with CC 3 cysteines and an exchangeable S-adenosyl-L-methionine (By CC similarity). CC -!- COFACTOR: Binds 1 2Fe-2S cluster. The cluster is coordinated with CC 3 cysteines and 1 arginine (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from CC 7,8-diaminononanoate: step 2/2. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin CC synthase family. 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; YP_001877111.1; -. DR SMR; B2UNW0; 17-319. DR GeneID; 6275395; -. DR GenomeReviews; CP001071_GR; Amuc_0492. DR KEGG; amu:Amuc_0492; -. DR HOGENOM; HBG405569; -. DR OMA; AGLEVCS; -. 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:HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:HAMAP. DR HAMAP; MF_01694; BioB; 1; -. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR010722; Biotin/thiamin_synth-assoc. DR InterPro; IPR002684; Biotin_synth. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; Radical_SAM. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Pfam; PF06968; BATS; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00876; BATS; 1. DR SMART; SM00729; Elp3; 1. PE 3: Inferred from homology; KW 2Fe-2S; 4Fe-4S; Biotin biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Metal-binding; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 321 Biotin synthase. FT /FTId=PRO_0000381189. FT METAL 62 62 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 66 66 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 69 69 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By FT similarity). FT METAL 106 106 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 138 138 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 198 198 Iron-sulfur 2 (2Fe-2S) (By similarity). FT METAL 268 268 Iron-sulfur 2 (2Fe-2S) (By similarity). 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 //