(data stored in ACNUC7421 zone)

SWISSPROT: BIOB_PSEAB

ID   BIOB_PSEAB              Reviewed;         352 AA.
AC   Q02TR6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 74.
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=PA14_06500;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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:0000255|HAMAP-Rule:MF_01694}.
CC   -!- CATALYTIC ACTIVITY: Dethiobiotin + sulfur-(sulfur carrier) + 2 S-
CC       adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin +
CC       (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2
CC       oxidized [2Fe-2S] ferredoxin. {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
CC       7,8-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
CC       synthase family. {ECO:0000255|HAMAP-Rule:MF_01694}.
DR   EMBL; CP000438; ABJ15462.1; -; Genomic_DNA.
DR   RefSeq; WP_003084824.1; NC_008463.1.
DR   ProteinModelPortal; Q02TR6; -.
DR   SMR; Q02TR6; -.
DR   EnsemblBacteria; ABJ15462; ABJ15462; PA14_06500.
DR   KEGG; pau:PA14_06500; -.
DR   HOGENOM; HOG000239957; -.
DR   KO; K01012; -.
DR   OMA; ADRFCMG; -.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000000653; 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-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
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   PANTHER; PTHR22976:SF32; PTHR22976:SF32; 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   TIGRFAMs; TIGR00433; bioB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02TR6.
DR   SWISS-2DPAGE; Q02TR6.
KW   2Fe-2S; 4Fe-4S; Biotin biosynthesis; Complete proteome; Iron;
KW   Iron-sulfur; Metal-binding; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    352       Biotin synthase.
FT                                /FTId=PRO_0000381554.
FT   METAL        59     59       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL        63     63       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL        66     66       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL       103    103       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL       134    134       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL       194    194       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
FT   METAL       266    266       Iron-sulfur 2 (2Fe-2S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01694}.
SQ   SEQUENCE   352 AA;  39140 MW;  1AD084B267718691 CRC64;
     MSATASVATR HDWSLAEVRA LFEQPFNDLL FQAQTVHRAY FDPNRVQVST LLSIKTGACP
     EDCKYCPQSG HYNTGLDKEK LMEVQKVLEA AAEAKAIGST RFCMGAAWKH PSAKDMPYVL
     EMVKGVKKLG LETCMTLGRL TQEQTQALAD AGLDYYNHNL DTSPEFYGNI ITTRTYSERL
     QTLAYVREAG MKICSGGILG MGESVDDRAG LLIQLANLPE HPESVPINML VKVKGTPLAE
     EKDVDPFDFI RTLAVARIMM PKSHVRLSAG REQMNEQMQA LAFMAGANSI FYGEKLLTTK
     NPQAEKDMQL FARLGIKPEE REEHADEVHQ AAIEQALVEQ RESKLFYNAA SA
//

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