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ID C8U1E9_ECO10 Unreviewed; 574 AA.
AC C8U1E9;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 08-MAY-2019, entry version 67.
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:BAI28957.1};
GN OrderedLocusNames=ECO103_0079 {ECO:0000313|EMBL:BAI28957.1};
OS Escherichia coli O103:H2 (strain 12009 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28957.1, ECO:0000313|Proteomes:UP000000959};
RN [1] {ECO:0000313|EMBL:BAI28957.1, ECO:0000313|Proteomes:UP000000959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA Hayashi T.;
RT "Comparative genomics reveal the mechanism of the parallel evolution
RT of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC Evidence={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; AP010958; BAI28957.1; -; Genomic_DNA.
DR RefSeq; WP_000425657.1; NC_013353.1.
DR EnsemblBacteria; BAI28957; BAI28957; ECO103_0079.
DR KEGG; eoh:ECO103_0079; -.
DR HOGENOM; HOG000258448; -.
DR KO; K01652; -.
DR OMA; MRSYNPV; -.
DR BioCyc; ECOL585395:ECO103_RS00400-MONOMER; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000000959; Chromosome.
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 CDD; cd02015; TPP_AHAS; 1.
DR InterPro; IPR012846; Acetolactate_synth_lsu.
DR InterPro; IPR039368; AHAS_TPP.
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;
DR PRODOM; C8U1E9.
DR SWISS-2DPAGE; C8U1E9.
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:UP000000959};
KW Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 5 168 TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT DOMAIN 196 330 TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT DOMAIN 394 545 TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ SEQUENCE 574 AA; 62945 MW; 946E0CFFD6234203 CRC64;
MEMLSGAEMV VRSLIDQGVK QVFGYPGGAV LDIYDALHTV GGIDHVLVRH EQAAVHMADG
LARATGEVGV VLVTSGPGAT NAITGIATAY MDSIPLVVLS GQVATSLIGY DAFQECDMVG
ISRPVVKHSF LVKQTEDIPQ VLKKAFWLAA SGRPGPVVVD LPKDILNPAN KLPYVWPESV
SMRSYNPTTT GHKGQIKRAL QTLVAAKKPV VYVGGGAIMA GCHQQLKETV EALNLPVVSS
LMGLGAFPAT HRQALGMLGM HGTYEANMTM HNADVIFAVG VRFDDRTTNN LAKYCPNATV
LHIDIDPTSI SKTVTADIPI VGDARQVLEQ MLELLSQESA HQPLDEIRDW WQQIEQWRAR
QCLKYDTHSE KIKPQAVIET LWRLTKGDAY VTSDVGQHQM FAALYYPFDK PRRWINSGGL
GTMGFGLPAA LGVKMALPEE TVVCVTGDGS IQMNIQELST ALQYELPVLV VNLNNRYLGM
VKQWQDMIYS GRHSQSYMQS LPDFVRLAEA YGHVGIQISH PHELESKLSE ALEQVCNNRL
VFVDVTVDGS EHVYPMQIRG GGMDEMWLSK TERT
//
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