(data stored in SCRATCH zone)

SWISSPROT: Q3Z5T3_SHISS

ID   Q3Z5T3_SHISS            Unreviewed;       574 AA.
AC   Q3Z5T3;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 100.
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:AAZ86879.1};
GN   OrderedLocusNames=SSON_0084 {ECO:0000313|EMBL:AAZ86879.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ86879.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ86879.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ86879.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ86879.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ86879; AAZ86879; SSON_0084.
DR   KEGG; ssn:SSON_0084; -.
DR   HOGENOM; HOG000258448; -.
DR   KO; K01652; -.
DR   OMA; MRSYNPV; -.
DR   BioCyc; SSON300269:G1GL2-96-MONOMER; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000002529; 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; Q3Z5T3.
DR   SWISS-2DPAGE; Q3Z5T3.
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:UP000002529};
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;  62949 MW;  4FE943692481B78C CRC64;
     MEMLSGAEMV VRSLIDQGVK QVFGYPGGAV LDIYDALHTV GGIDHVLVRH EQAAVHMADG
     LARATGEVGV VLVTSGPGAT NAITGIATAY MDSIPLVVLS GQVATSLIGY DAFQECDMVG
     ISRPVVKHSF LVKQTEDIPQ VLKKAFWLAA SGRPGPVVVD LPKDILNPAN KLPYVWPESV
     SMRSYNPTTT GHKGQIKRAL QTLVAAKKPV VYVGGGAITA 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 ALEQVHNNRL
     VFVDVTVDGS EHVYPMQIRG GGMDEMWLSK TERT
//

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