(data stored in SCRATCH zone)

SWISSPROT: BIOB_SYNS3

ID   BIOB_SYNS3              Reviewed;         328 AA.
AC   Q0IBC8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   11-DEC-2019, entry version 84.
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=sync_1032;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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=[sulfur carrier]-SH + dethiobiotin + 2 reduced [2Fe-2S]-
CC         [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:57861, ChEBI:CHEBI:59789, ChEBI:CHEBI:64428; 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   -!- SEQUENCE CAUTION:
CC       Sequence=ABI46705.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000435; ABI46705.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041426446.1; NC_008319.1.
DR   SMR; Q0IBC8; -.
DR   STRING; 64471.sync_1032; -.
DR   PRIDE; Q0IBC8; -.
DR   EnsemblBacteria; ABI46705; ABI46705; sync_1032.
DR   KEGG; syg:sync_1032; -.
DR   eggNOG; ENOG4107QSQ; Bacteria.
DR   eggNOG; COG0502; LUCA.
DR   HOGENOM; HOG000239957; -.
DR   KO; K01012; -.
DR   OrthoDB; 940969at2; -.
DR   BioCyc; SSP64471:G1G72-981-MONOMER; -.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000001961; 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; SFLDF00272; biotin_synthase; 1.
DR   SMART; SM00876; BATS; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00433; bioB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0IBC8.
DR   SWISS-2DPAGE; Q0IBC8.
KW   2Fe-2S; 4Fe-4S; Biotin biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..328
FT                   /note="Biotin synthase"
FT                   /id="PRO_0000381680"
FT   METAL           57
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           61
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           64
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           101
FT                   /note="Iron-sulfur 2 (2Fe-2S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           133
FT                   /note="Iron-sulfur 2 (2Fe-2S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           193
FT                   /note="Iron-sulfur 2 (2Fe-2S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   METAL           265
FT                   /note="Iron-sulfur 2 (2Fe-2S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
SQ   SEQUENCE   328 AA;  35594 MW;  CC9BBA7C80CD4E97 CRC64;
     MTEAVEVRHD WTRSEIEALL DLPLMDLLWR AQGVHRASNP GYHVQLASLL SVKTGGCEED
     CAYCPQSMHH SSDVTGQPEL QVAPVLERAK AAKQAGADRF CMGWAWREIR DGAPFEAMLQ
     MVSGVRALGM EACVTAGMLT DGQAQRLAKA GLTAYNHNLD TSPEHYDKII TTRTFQERLE
     TLERVRQAGV TLCCGGIIGM GETIGDRASM LQVLASINPH PESVPINALV AVEGTPLEEL
     PPIDPIELVR MIAVTRILMP GSRVRLSAGR EQLSKEAQIL CLQAGADSIF YGETLLTTGN
     PAVEADRELL RTAGVQANWL SASEKLAA
//

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