ID   BIOB_BRADU              Reviewed;         331 AA.
AC   Q9AMS7; Q79UC4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 133.
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};
GN   OrderedLocusNames=blr2095; ORFNames=id897;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=USDA 110spc4;
RX   PubMed=11157954; DOI=10.1128/jb.183.4.1405-1412.2001;
RA   Goettfert M., Roethlisberger S., Kuendig C., Beck C., Marty R.,
RA   Hennecke H.;
RT   "Potential symbiosis-specific genes uncovered by sequencing a 410-kb DNA
RT   region of the Bradyrhizobium japonicum chromosome.";
RL   J. Bacteriol. 183:1405-1412(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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}.
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DR   EMBL; AH010242; AAG61070.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC47360.1; -; Genomic_DNA.
DR   RefSeq; NP_768735.1; NC_004463.1.
DR   RefSeq; WP_011084890.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q9AMS7; -.
DR   SMR; Q9AMS7; -.
DR   STRING; 224911.AAV28_07305; -.
DR   EnsemblBacteria; BAC47360; BAC47360; BAC47360.
DR   GeneID; 83557770; -.
DR   KEGG; bja:blr2095; -.
DR   PATRIC; fig|224911.44.peg.1604; -.
DR   eggNOG; COG0502; Bacteria.
DR   HOGENOM; CLU_033172_1_2_5; -.
DR   InParanoid; Q9AMS7; -.
DR   OrthoDB; 9786826at2; -.
DR   PhylomeDB; Q9AMS7; -.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004076; F:biotin synthase activity; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
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; SFLDF00272; biotin_synthase; 1.
DR   SFLD; SFLDG01278; biotin_synthase_like; 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..331
FT                   /note="Biotin synthase"
FT                   /id="PRO_0000381244"
FT   DOMAIN          53..272
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         68
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         75
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         112
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   BINDING         143
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   BINDING         203
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   BINDING         276
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
SQ   SEQUENCE   331 AA;  36011 MW;  BE11557840FC5B3F CRC64;
     MDAAVQVQRK KASNGAQVRN HWNVEEAKAL YDLPFADLML QAQRAHRKNF DPNHVETASL
     LSIKTGGCPE DCGYCSQSAH YATGLKATRL MRCADVVATA QRAKDAGATR FCMAAAWRTP
     KDRDLDSVCD MVNAVKGLGM ETCVTLGTLT PKHAARLAEA GLDFYNHNVD TSPEFYSKII
     TTRSLQDRID TLAHVRDAGI KICCGGIIGM GERVEDRLGM LVLLANLPNY PESVPINLWN
     KIEGVPVEDT AEPPDPIALV RLLATARVMM PRSVVRLSAG RQYMTDELQA LCFLAGANSI
     FVGDVLLTTN NPKVDRDADL LARLGITSGL A
//