ID   ILVM_ECOLI              Reviewed;          87 AA.
AC   P0ADG1; P13048; P78269; Q2M878;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   24-JAN-2024, entry version 117.
DE   RecName: Full=Acetolactate synthase isozyme 2 small subunit;
DE            EC=2.2.1.6;
DE   AltName: Full=ALS-II;
DE   AltName: Full=Acetohydroxy-acid synthase II small subunit;
DE            Short=AHAS-II;
GN   Name=ilvM; OrderedLocusNames=b3769, JW3742;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3897211; DOI=10.1093/oxfordjournals.jbchem.a135176;
RA   Kuramitsu S., Ogawa T., Ogawa H., Kagamiyama H.;
RT   "Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide
RT   sequence of the ilvE gene and the deduced amino acid sequence.";
RL   J. Biochem. 97:993-999(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=K12;
RX   PubMed=3550695; DOI=10.1093/nar/15.5.2137;
RA   Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E.,
RA   Hatfield G.W.;
RT   "The complete nucleotide sequence of the ilvGMEDA operon of Escherichia
RT   coli K-12.";
RL   Nucleic Acids Res. 15:2137-2155(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1569580; DOI=10.1016/0022-2836(92)90460-2;
RA   Pagel J.M., Winkelman J.W., Adams C.W., Hatfield G.W.;
RT   "DNA topology-mediated regulation of transcription initiation from the
RT   tandem promoters of the ilvGMEDA operon of Escherichia coli.";
RL   J. Mol. Biol. 224:919-935(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=1379743; DOI=10.1126/science.1379743;
RA   Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT   84.5 to 86.5 minutes.";
RL   Science 257:771-778(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
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: Tetramer of two large and two small chains.
CC   -!- INTERACTION:
CC       P0ADG1; P0DP90: ilvG; NbExp=2; IntAct=EBI-1133722, EBI-1133701;
CC   -!- MISCELLANEOUS: E.coli contains genes for 3 AHAS isozymes: ilvBN, ilvGM
CC       and ilvIH.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB59051.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA26261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X02413; CAA26261.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M10313; AAB59051.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X04890; CAA28574.1; -; Genomic_DNA.
DR   EMBL; M87049; AAA67572.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77489.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77528.1; -; Genomic_DNA.
DR   RefSeq; NP_418217.1; NC_000913.3.
DR   RefSeq; WP_000983255.1; NZ_STEB01000021.1.
DR   AlphaFoldDB; P0ADG1; -.
DR   SMR; P0ADG1; -.
DR   BioGRID; 4263292; 7.
DR   BioGRID; 852581; 1.
DR   ComplexPortal; CPX-3570; Acetolactate synthase II complex.
DR   IntAct; P0ADG1; 4.
DR   STRING; 511145.b3769; -.
DR   PaxDb; 511145-b3769; -.
DR   EnsemblBacteria; AAC77489; AAC77489; b3769.
DR   GeneID; 83578692; -.
DR   GeneID; 948279; -.
DR   KEGG; ecj:JW3742; -.
DR   KEGG; eco:b3769; -.
DR   PATRIC; fig|1411691.4.peg.2937; -.
DR   EchoBASE; EB0496; -.
DR   eggNOG; COG3978; Bacteria.
DR   HOGENOM; CLU_183627_0_0_6; -.
DR   InParanoid; P0ADG1; -.
DR   OMA; RGFQICS; -.
DR   OrthoDB; 6198158at2; -.
DR   PhylomeDB; P0ADG1; -.
DR   BioCyc; EcoCyc:SMALLILVM-MONOMER; -.
DR   BRENDA; 2.2.1.6; 2026.
DR   SABIO-RK; P0ADG1; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   PRO; PR:P0ADG1; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005948; C:acetolactate synthase complex; IPI:ComplexPortal.
DR   GO; GO:0003984; F:acetolactate synthase activity; IDA:EcoCyc.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IDA:EcoCyc.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IDA:ComplexPortal.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.70.260; -; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   Pfam; PF13710; ACT_5; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Direct protein sequencing; Magnesium; Reference proteome;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..87
FT                   /note="Acetolactate synthase isozyme 2 small subunit"
FT                   /id="PRO_0000151429"
FT   DOMAIN          5..78
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   87 AA;  9703 MW;  CEB6B5211262E0AF CRC64;
     MMQHQVNVSA RFNPETLERV LRVVRHRGFH VCSMNMAAAS DAQNINIELT VASPRSVDLL
     FSQLNKLVDV AHVAICQSTT TSQQIRA
//