(data stored in SCRATCH zone)

SWISSPROT: A0A0H3JBR8_ECO57

ID   A0A0H3JBR8_ECO57        Unreviewed;       588 AA.
AC   A0A0H3JBR8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 16.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   OrderedLocusNames=ECs0081 {ECO:0000313|EMBL:BAB33504.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB33504.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB33504.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
CC       {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:RU362132}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BA000007; BAB33504.1; -; Genomic_DNA.
DR   RefSeq; NP_308108.2; NC_002695.1.
DR   ProteinModelPortal; A0A0H3JBR8; -.
DR   STRING; 155864.Z0087; -.
DR   EnsemblBacteria; BAB33504; BAB33504; BAB33504.
DR   GeneID; 913521; -.
DR   KEGG; ecs:ECs0081; -.
DR   PATRIC; fig|386585.9.peg.181; -.
DR   KO; K01652; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000000558; 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   Gene3D; 3.40.50.1220; -; 1.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
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; A0A0H3JBR8.
DR   SWISS-2DPAGE; A0A0H3JBR8.
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:UP000000558};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN       19    182       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      210    344       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      408    559       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   588 AA;  64597 MW;  E843380DCEC4D1DB CRC64;
     MCFTHFFRQT VRQAMEMLSG AEMVVRSLID QGVKQVFGYP GGAVLDIYDA LHTVGGIGHV
     LVRHEQAAVH MADGLARATG EVGVVLVTSG PGATNAITGI ATAYMDSIPL VVLSGQVATS
     LIGYDAFQEC DMVGISRPVV KHSFLVKQTE DIPQVLKKAF WLAASGRPGP VVVDLPKDIL
     NPANKLPYVW PESVSMRSYN PTTTGHKGQI KRALQTLVAA KKPVVYVGGG AITAGCHQQL
     KETVEALNLP VVSSLMGLGA FPATHRQALG MLGMHGTYEA NMTMHNADVI FAVGVRFDDR
     TTNNLAKYCP NATVLHIDID PTSISKTVTA DIPIVGDARQ VLEQMLELLS QESAHQPLDE
     IRDWWQQIEQ WRARQCLKYD THSEKIKPQA VIETLWRLTK GGAYVTSDVG QHQMFAALYY
     PFDKPRRWIN SGGLGTMGFG LPAALGVKMA LPEETVVCVT GDGSIQMNIQ ELSTALQYEL
     PVLVVNLNNR YLGMVKQWQD MIYSGRHSQS YMQSLPDFVR LAEAYGHVGI QISHPQELES
     KLSEALEQVR NNRLVFVDVT VDGSEHVYPM QIRGGGMDEM WLSKTERT
//

If you have problems or comments...

PBIL Back to PBIL home page