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Database: UniProt/TrEMBL
Entry: C9X9R4_SALTD
LinkDB: C9X9R4_SALTD
Original site: C9X9R4_SALTD 
ID   C9X9R4_SALTD            Unreviewed;       548 AA.
AC   C9X9R4;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   11-JUN-2014, entry version 33.
DE   RecName: Full=Acetolactate synthase;
DE            EC=2.2.1.6;
GN   OrderedLocusNames=STMMW_38761;
OS   Salmonella typhimurium (strain D23580).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=568708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D23580;
RX   PubMed=19901036; DOI=10.1101/gr.091017.109;
RA   Kingsley R.A., Msefula C.L., Thomson N.R., Kariuki S., Holt K.E.,
RA   Gordon M.A., Harris D., Clarke L., Whitehead S., Sangal V., Marsh K.,
RA   Achtman M., Molyneux M.E., Cormican M., Parkhill J., Maclennan C.A.,
RA   Heyderman R.S., Dougan G.;
RT   "Epidemic multiple drug resistant Salmonella typhimurium causing
RT   invasive disease in sub-Saharan Africa have a distinct genotype.";
RL   Genome Res. 19:2279-2287(2009).
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC       similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 1/4.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
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DR   EMBL; FN424405; CBG26889.1; -; Genomic_DNA.
DR   RefSeq; YP_005234884.1; NC_016854.1.
DR   ProteinModelPortal; C9X9R4; -.
DR   PRIDE; C9X9R4; -.
DR   EnsemblBacteria; CBG26889; CBG26889; STMMW_38761.
DR   PATRIC; 36729507; VBISalEnt111430_4140.
DR   HOGENOM; HOG000258448; -.
DR   BioCyc; SENT568708:GJDP-3939-MONOMER; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
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:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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   Gene3D; 3.40.50.970; -; 2.
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; IPR000399; TPP-bd_CS.
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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Magnesium; Metal-binding; Thiamine pyrophosphate;
KW   Transferase.
SQ   SEQUENCE   548 AA;  59224 MW;  6587AAE9E6E2BE04 CRC64;
     MNGAQWVVHA LRAQGVKTVF GYPGGAIMPV YDALYDGGVE HLLCRHEQGA AMAAIGYARS
     TGKTGVCIAT SGPGATNLIT GLADALLDSV PVVAITGQVS APFIGTDAFQ EVDVLGLSLA
     CTKHSFLVQS LEELPRIMAE AFEVANAGRP GPVLVDIPKD IQLASGELEP WFTTVANEAT
     FPQADVEQAR QMLEQAKKPM LYVGGGVGMA QAVPALRKFI AVTQMPVTCT LKGLGAVEAD
     YPYYLGMLGM HGTKAANFAV QECDLLIAVG ARFDDRVTGK LNTFAPNASV IHMDIDPAEM
     NKLRQAHVAL QGDLNSLLPA LQQPLKIDAW RQSCAELRAE HAWRYDHPGE TIYAPLLLKQ
     LSERKPADSV VTTDVGQHQM WSAQHMTYTR PENFITSSGL GTMGFGLPAA VGAQVARPND
     TVICISGDGS FMMNVQELGT VKRKQLPLKI VLLDNQRLGM VRQWQQLFFQ ERYSETTLTD
     NPDFLMLASA FGIPGQHITR KDQVEAALDT MLASEGPYLL HVSIDELENV WPLVPPGASN
     SEMLEKLS
//
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