ID   ILVN_ECOL6              Reviewed;          96 AA.
AC   P0ADF9; P08143;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Acetolactate synthase isozyme 1 small subunit;
DE            EC=2.2.1.6;
DE   AltName: Full=Acetohydroxy-acid synthase I small subunit;
DE            Short=AHAS-I;
DE            Short=ALS-I;
GN   Name=ilvN; OrderedLocusNames=c4595;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4.
CC   -!- SUBUNIT: Dimer of large and small chains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AE014075; AAN83029.1; -; Genomic_DNA.
DR   RefSeq; WP_001181706.1; NC_004431.1.
DR   AlphaFoldDB; P0ADF9; -.
DR   BMRB; P0ADF9; -.
DR   SMR; P0ADF9; -.
DR   STRING; 199310.c4595; -.
DR   EnsemblBacteria; AAN83029; AAN83029; c4595.
DR   GeneID; 66672433; -.
DR   KEGG; ecc:c4595; -.
DR   eggNOG; COG0440; Bacteria.
DR   HOGENOM; CLU_165363_0_0_6; -.
DR   OMA; NEQSRIW; -.
DR   BioCyc; ECOL199310:C4595-MON; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000001410; Chromosome.
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   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; PTHR30239; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Transferase.
FT   CHAIN           1..96
FT                   /note="Acetolactate synthase isozyme 1 small subunit"
FT                   /id="PRO_0000151421"
FT   DOMAIN          10..83
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   96 AA;  11106 MW;  7F37DD421EDD3802 CRC64;
     MQNTTHDNVI LELTVRNHPG VMTHVCGLFA RRAFNVEGIL CLPIQDSDKS HIWLLVNDDQ
     RLEQMISQID KLEDVVKVQR NQSDPTMFNK IAVFFQ