(data stored in SCRATCH zone)

SWISSPROT: C8U1E9_ECO10

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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