ID A0A062WNJ5_9ACTN Unreviewed; 363 AA. AC A0A062WNJ5; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-OCT-2020, entry version 32. DE RecName: Full=Biotin synthase {ECO:0000256|ARBA:ARBA00012236, ECO:0000256|HAMAP-Rule:MF_01694}; DE EC=2.8.1.6 {ECO:0000256|ARBA:ARBA00012236, ECO:0000256|HAMAP-Rule:MF_01694}; GN Name=bioB {ECO:0000256|HAMAP-Rule:MF_01694}; GN ORFNames=BMG523Draft_03731 {ECO:0000313|EMBL:KDA41472.1}; OS Frankia sp. BMG5.23. OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia; OC unclassified Frankia. OX NCBI_TaxID=683305 {ECO:0000313|EMBL:KDA41472.1, ECO:0000313|Proteomes:UP000027007}; RN [1] {ECO:0000313|EMBL:KDA41472.1, ECO:0000313|Proteomes:UP000027007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BMG5.23 {ECO:0000313|EMBL:KDA41472.1, RC ECO:0000313|Proteomes:UP000027007}; RA Hurst S.G.IV., Ghodhbane-Gtari F., Oshone R., Morris K., Thomas K., RA Abebe-Akele F., Gtari M., Tisa L.S.; RT "Draft Genome of BMG5.23."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|ARBA:ARBA00023417, ECO:0000256|HAMAP- CC Rule:MF_01694}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8- CC diaminononanoate: step 2/2. {ECO:0000256|ARBA:ARBA00004942, CC ECO:0000256|HAMAP-Rule:MF_01694}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01694}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase CC family. {ECO:0000256|ARBA:ARBA00010765, ECO:0000256|HAMAP- CC Rule:MF_01694}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KDA41472.1}. 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; JDWE01000048; KDA41472.1; -; Genomic_DNA. DR EnsemblBacteria; KDA41472; KDA41472; BMG523Draft_03731. DR PATRIC; fig|683305.3.peg.3814; -. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000027007; Unassembled WGS sequence. 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 SMART; SM00876; BATS; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00433; bioB; 1. PE 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|PIRSR:PIRSR001619-1}; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|PIRSR:PIRSR001619-1}; KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756, ECO:0000256|HAMAP- KW Rule:MF_01694}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|PIRSR:PIRSR001619-1}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_01694, ECO:0000256|PIRSR:PIRSR001619-1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01694, ECO:0000256|PIRSR:PIRSR001619-1}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_01694, ECO:0000256|PIRSR:PIRSR001619-1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000313|EMBL:KDA41472.1}. FT DOMAIN 61..267 FT /note="Elp3" FT /evidence="ECO:0000259|SMART:SM00729" FT DOMAIN 238..328 FT /note="BATS" FT /evidence="ECO:0000259|SMART:SM00876" FT METAL 71 FT /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT METAL 75 FT /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT METAL 78 FT /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT METAL 115 FT /note="Iron-sulfur 2 (2Fe-2S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT METAL 148 FT /note="Iron-sulfur 2 (2Fe-2S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT METAL 208 FT /note="Iron-sulfur 2 (2Fe-2S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" FT METAL 278 FT /note="Iron-sulfur 2 (2Fe-2S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694, FT ECO:0000256|PIRSR:PIRSR001619-1" SQ SEQUENCE 363 AA; 38606 MW; E0051CB21DD826C2 CRC64; MTDMDLSATL NSLVSKGVSG QAPTRDEALA VLRSDDDDLL DVVAAAYRLR RRYFGRRVKL NFLVNLKSGL CPEDCSYCSQ RLGSNTGILK YTWLKPEEAA ATAGAGISGG ARRVCLVASG RGPTDRDVDR VADTIGAIKT AHPDVEVCAC LGLLSDGQAA QLRAAGADAY NHNLNTAGEK YADICTTHTY NDRVDTVQEA RHAGLSPCSG IIAGMGESDE DLVDVAFALR ELAPDSIPVN FLMPFEGTPL GAEWNLNPRQ CLRILAMVRF VNPTAEVRLS GGREIHLGSM QPLALSVVNS IFLGDYLTSE GQEGHQDLKM IAEAGFTVEG LNTDAEAALA MGAGLERVAL RQRGAGTDLP PNA //