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Database: UniProt
Entry: Q63VP8_BURPS
LinkDB: Q63VP8_BURPS
Original site: Q63VP8_BURPS 
ID   Q63VP8_BURPS            Unreviewed;       587 AA.
AC   Q63VP8;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   20-DEC-2017, entry version 81.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   Name=ilvI {ECO:0000313|EMBL:CAH35191.1};
GN   OrderedLocusNames=BPSL1196 {ECO:0000313|EMBL:CAH35191.1};
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH35191.1, ECO:0000313|Proteomes:UP000000605};
RN   [1] {ECO:0000313|EMBL:CAH35191.1, ECO:0000313|Proteomes:UP000000605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243 {ECO:0000313|EMBL:CAH35191.1,
RC   ECO:0000313|Proteomes:UP000000605};
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.,
RA   Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R.,
RA   Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I.,
RA   Chillingworth T., Cronin A., Crosset B., Davis P., DeShazer D.,
RA   Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K.,
RA   Keith K.E., Maddison M., Moule S., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis,
RT   Burkholderia pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 Mg(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 1/4. {ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU003591}.
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DR   EMBL; BX571965; CAH35191.1; -; Genomic_DNA.
DR   RefSeq; WP_004522422.1; NZ_CP009538.1.
DR   RefSeq; YP_107818.1; NC_006350.1.
DR   ProteinModelPortal; Q63VP8; -.
DR   STRING; 272560.BPSL1196; -.
DR   EnsemblBacteria; CAH35191; CAH35191; BPSL1196.
DR   GeneID; 3093947; -.
DR   KEGG; bps:BPSL1196; -.
DR   PATRIC; fig|272560.51.peg.331; -.
DR   eggNOG; ENOG4105C7K; Bacteria.
DR   eggNOG; COG0028; LUCA.
DR   HOGENOM; HOG000258448; -.
DR   KO; K01652; -.
DR   OMA; MRSYNPV; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00118; acolac_lg; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU003591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000605};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591,
KW   ECO:0000313|EMBL:CAH35191.1}.
FT   DOMAIN       23    188       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      211    347       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      410    558       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   587 AA;  64866 MW;  C2236A6FEF1E9ECD CRC64;
     MNMPSAEFST SESLSPQKTG SIGATVLMKA LADENVEFIW GYPGGSVLYI YDELYKQDKI
     QHVLVRHEQA AVHAADAYSR STGKVGVCLV TSGPGVTNAV TGIATAYMDS IPLVVISGQV
     PTAAIGQDAF QECDTVGITR PCVKHNFLVK DVRELAQTVK KAFYIARTGR PGPVLIDIPK
     DISKTPCEYE PVKNVSLRSY NPVTKGHSGQ IRKAVSLLLS AKRPYIYTGG GIILADASRE
     LNQFADLLGY PVTNTLMGLG GYRSSDRKFL GMLGMHGTYE ANMAMQHCDV LIAIGARFDD
     RVIGDPAHFA SRPRKIIHID IDPSSISKRV KVDIPIVGDV KEVLKELIEQ LQTAEHGPDA
     DALAQWWKEI EGWRGTDCLK YDRASEIIKP QYVVEKLWEL TDGNAFVCSD VGQHQMWAAQ
     FYRFNKPRRW INSGGLGTMG FGLPAAMGVK MAHPDDDVVC ITGEGSIQMC IQELSTCKQY
     DTPVKIISLN NRYLGMVRQW QQIEYSKRYS HSYMDALPDF VKLAQAYGHI GMRIEKSADV
     EPALKEALSL KDRTVFLDFQ TDPTENVWPM VQAGKGITEM LLGSEDL
//
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