ID C9X9R4_SALTD Unreviewed; 548 AA.
AC C9X9R4;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 01-MAY-2013, entry version 28.
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 GeneID; 11762907; -.
DR KEGG; sev:STMMW_38761; -.
DR PATRIC; 36729507; VBISalEnt111430_4140.
DR HOGENOM; HOG000258448; -.
DR KO; K01652; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA: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 InterPro; IPR012846; Acetolactate_synth_lsu.
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 PANTHER; PTHR18968:SF13; PTHR18968:SF13; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
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
//
