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Database: UniProt
Entry: G5QAA2_SALMO
LinkDB: G5QAA2_SALMO
Original site: G5QAA2_SALMO 
ID   G5QAA2_SALMO            Unreviewed;        96 AA.
AC   G5QAA2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE            EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN   ORFNames=LTSEMON_5394 {ECO:0000313|EMBL:EHC73232.1};
OS   Salmonella enterica subsp. enterica serovar Montevideo str. S5-403.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913242 {ECO:0000313|EMBL:EHC73232.1, ECO:0000313|Proteomes:UP000003221};
RN   [1] {ECO:0000313|EMBL:EHC73232.1, ECO:0000313|Proteomes:UP000003221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5-403 {ECO:0000313|EMBL:EHC73232.1,
RC   ECO:0000313|Proteomes:UP000003221};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
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|ARBA:ARBA00000673};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004974}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC   -!- SUBUNIT: Dimer of large and small chains.
CC       {ECO:0000256|ARBA:ARBA00011744}.
CC   -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC       {ECO:0000256|ARBA:ARBA00006341}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHC73232.1}.
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DR   EMBL; AFCS01001199; EHC73232.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5QAA2; -.
DR   PATRIC; fig|913242.3.peg.4688; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000003221; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04878; ACT_AHAS; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   InterPro; IPR004789; Acetalactate_synth_ssu.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR039557; AHAS_ACT.
DR   PANTHER; PTHR30239:SF4; ACETOLACTATE SYNTHASE ISOZYME 1 SMALL SUBUNIT; 1.
DR   PANTHER; PTHR30239; ACETOLACTATE SYNTHASE SMALL SUBUNIT; 1.
DR   Pfam; PF13710; ACT_5; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Coiled coil {ECO:0000256|SAM:Coils}.
FT   DOMAIN          10..83
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   COILED          55..82
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   96 AA;  11038 MW;  EB1BC44E6994E4CE CRC64;
     MQKQSHDNVI LELTVRNHPG VMTHVCGLFA RRAFNVEGIL CLPIQGSDQS RIWLLVNDDQ
     RLEQMISQID KLEDVAKVVR NQSDPTMFNK IAVFFE
//
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