ID A0A062WNJ5_9ACTO Unreviewed; 363 AA. AC A0A062WNJ5; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JAN-2015, entry version 5. DE RecName: Full=Biotin synthase {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|SAAS:SAAS00063351}; DE EC=2.8.1.6 {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|SAAS:SAAS00063265}; 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; Actinobacteridae; Actinomycetales; OC Frankineae; Frankiaceae; Frankia. OX NCBI_TaxID=683305 {ECO:0000313|EMBL:KDA41472.1}; RN [1] {ECO:0000313|EMBL:KDA41472.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BMG5.23 {ECO:0000313|EMBL:KDA41472.1}; 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 CC by the insertion of a sulfur atom into dethiobiotin via a radical- CC based mechanism. {ECO:0000256|HAMAP-Rule:MF_01694, CC ECO:0000256|SAAS:SAAS00063284}. CC -!- CATALYTIC ACTIVITY: Dethiobiotin + sulfur-(sulfur carrier) + 2 S- CC adenosyl-L-methionine = biotin + (sulfur carrier) + 2 L-methionine CC + 2 5'-deoxyadenosine. {ECO:0000256|HAMAP-Rule:MF_01694, CC ECO:0000256|SAAS:SAAS00063349}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01694}; CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 CC cysteines and 1 arginine. {ECO:0000256|HAMAP-Rule:MF_01694}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000256|SAAS:SAAS00170433}; CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 CC cysteines and 1 arginine. {ECO:0000256|SAAS:SAAS00170433}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01694}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|SAAS:SAAS00170439}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|SAAS:SAAS00170439}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from CC 7,8-diaminononanoate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01694, CC ECO:0000256|SAAS:SAAS00063342}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01694, CC ECO:0000256|SAAS:SAAS00063319}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin CC synthase family. {ECO:0000256|HAMAP-Rule:MF_01694}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. 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 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|HAMAP-Rule:MF_01694, KW ECO:0000256|SAAS:SAAS00063334}; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|SAAS:SAAS00063352}; KW Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|SAAS:SAAS00063242}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|SAAS:SAAS00063343}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|SAAS:SAAS00063338}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|SAAS:SAAS00063322}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|SAAS:SAAS00063330}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01694, KW ECO:0000256|SAAS:SAAS00063301}. FT METAL 71 71 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01694}. FT METAL 75 75 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01694}. FT METAL 78 78 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01694}. FT METAL 115 115 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000256|HAMAP-Rule:MF_01694}. FT METAL 148 148 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000256|HAMAP-Rule:MF_01694}. FT METAL 208 208 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000256|HAMAP-Rule:MF_01694}. FT METAL 278 278 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000256|HAMAP-Rule:MF_01694}. 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 //