(data stored in SCRATCH zone)

SWISSPROT: C5BBA2_EDWI9

ID   C5BBA2_EDWI9            Unreviewed;       549 AA.
AC   C5BBA2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   OrderedLocusNames=NT01EI_0077 {ECO:0000313|EMBL:ACR67337.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67337.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001600; ACR67337.1; -; Genomic_DNA.
DR   RefSeq; WP_015869558.1; NC_012779.2.
DR   ProteinModelPortal; C5BBA2; -.
DR   STRING; 634503.NT01EI_0077; -.
DR   EnsemblBacteria; ACR67337; ACR67337; NT01EI_0077.
DR   GeneID; 7959796; -.
DR   KEGG; eic:NT01EI_0077; -.
DR   PATRIC; fig|634503.3.peg.70; -.
DR   eggNOG; ENOG4105C7K; Bacteria.
DR   eggNOG; COG0028; LUCA.
DR   HOGENOM; HOG000258448; -.
DR   KO; K01652; -.
DR   OMA; FRPLCKF; -.
DR   OrthoDB; POG091H02KO; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000001485; 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; C5BBA2.
DR   SWISS-2DPAGE; C5BBA2.
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:UP000001485};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|RuleBase:RU003591,
KW   ECO:0000313|EMBL:ACR67337.1}.
FT   DOMAIN        1    165       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      188    322       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      375    523       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   549 AA;  58203 MW;  796D3FC127C1A142 CRC64;
     MNGAQWVVQA LRAQGVNQVF GYPGGAIMPL YDALYDGGVA HLLCRHEQGA VMAAIGYARA
     SGRVGVCIAT SGPGATNLIT GLADAMMDSV PLVAITGQVA SALIGTDAFQ EMDVLGLSLA
     CTKHSFMVTS LAELPEVMDR AFAIAVQGRP GPVLIDIPKD IQLAQGDLAT PLCSVAQVQP
     SCPPAALAQA RAMLTQAQRP VLYVGGGVGM AGAVPSLRSL VSRSGMPVAA TLKGLGAADD
     RHPAYLGMLG MHGCKAANLA VQQCDLLIAV GARFDDRVTG RLDAFAPQAQ VIHLDIDPAE
     LGKVRQAHVS LCGDLNLLLS ALTMRLEIAP WLQQVAALKA QHAWRYDHPG EAIYAPLFLR
     QLSGCKPPQA VVTTDVGQHQ MWSAQHMRFS LPQDFITSSG LGTMGFGIPA AVGAQVARPD
     DCVICVSGDG SFMMNVQELG TIKRARLPLK IVLLDNQRLG MVRQWQQLFF DARYSETDLS
     DNPDFLTLAQ AFGIPGQRIS RKAQVAEALE ALFSTPGPYL LQVAIDEFEN VWPLVPPGAG
     NESMLENVS
//

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