ID   ILVM_SHIFL              Reviewed;          87 AA.
AC   P0ADG3; P13048; P78269;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   25-MAY-2022, entry version 101.
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=SF3844, S3915;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN45281.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAP18916.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN45281.2; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP18916.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_709574.2; NC_004337.2.
DR   RefSeq; WP_000983255.1; NZ_WPGW01000028.1.
DR   AlphaFoldDB; P0ADG3; -.
DR   SMR; P0ADG3; -.
DR   STRING; 198214.SF3844; -.
DR   EnsemblBacteria; AAN45281; AAN45281; SF3844.
DR   EnsemblBacteria; AAP18916; AAP18916; S3915.
DR   GeneID; 1025509; -.
DR   GeneID; 67414443; -.
DR   KEGG; sfl:SF3844; -.
DR   KEGG; sfx:S3915; -.
DR   PATRIC; fig|198214.7.peg.4535; -.
DR   HOGENOM; CLU_183627_0_0_6; -.
DR   OrthoDB; 2080824at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Magnesium;
KW   Reference proteome; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..87
FT                   /note="Acetolactate synthase isozyme 2 small subunit"
FT                   /id="PRO_0000151431"
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