ID Q0WJC7_YERPE Unreviewed; 575 AA.
AC Q0WJC7;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 01-MAY-2013, entry version 57.
DE RecName: Full=Acetolactate synthase;
DE EC=2.2.1.6;
GN Name=ilvI; OrderedLocusNames=YPO0539;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G.,
RA Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V.,
RA Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M.,
RA Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
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; AL590842; CAL19219.1; -; Genomic_DNA.
DR PIR; AI0066; AI0066.
DR RefSeq; YP_002345611.1; NC_003143.1.
DR ProteinModelPortal; Q0WJC7; -.
DR STRING; 214092.YPO0539; -.
DR GeneID; 1173384; -.
DR KEGG; ype:YPO0539; -.
DR PATRIC; 18590186; VBIYerPes7843_0830.
DR HOGENOM; HOG000258448; -.
DR KO; K01652; -.
DR OMA; GRYEANM; -.
DR ProtClustDB; PRK07979; -.
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; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
SQ SEQUENCE 575 AA; 62731 MW; 3F3E10E4EAFC2FCA CRC64;
MEMLSGAEMV VRSLIDQGVK HVFGYPGGAV LDIYDALHTV GGIDHVLVRH EQGAVHMADG
YARATGEVGV VLVTSGPGAT NAITGIATAY MDSVPMVVLS GQVPSSLIGF DAFQECDMVG
ISRPVVKHSF LVKRTEDIPM VLKKAFYLAS TGRPGPVVID LPKDIVGPAV KMPYAYPEQV
SLRSYNPTVQ GHRGQIKRAL QTIMAAKRPI MYVGGGAINA ACHEELLILA EKLNLPVTSS
LMGLGSFPGT HRQSVGMLGM HGTFEANMAM HNTDLIFAVG VRFDDRTTNN LAKYCPDATV
LHIDIDPTSI SKTVTADIPI VGDAKQVLTQ MLDLLSQVGC TQDFDSLRDW WQSIEQWRTR
NCLGYNKDSG KIKPQAVIEA LHRLTKGDAY VTSDVGQHQM FAALYYPFDK PRRWINSGGL
GTMGFGLPAA LGVKLALPNE TVVCVTGDGS IQMNIQELST ALQYNLPVLV LNLNNRYLGM
VKQWQDMIYS GRHSQSYMDS LPDFVKLAEA YGHIGVAINT PDELESKLAD ALTQLSETNR
LVFVDVTVDE TEHVYPMQIR GGGMDEMWLS KTERT
//
