ID   ILVH_MYCTO              Reviewed;         168 AA.
AC   P9WKJ2; L0TE14; O53249; P65161;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Putative acetolactate synthase small subunit;
DE            EC=2.2.1.6;
DE   AltName: Full=Acetohydroxy-acid synthase small subunit;
DE            Short=AHAS;
DE            Short=ALS;
GN   Name=ilvH; Synonyms=ilvN; OrderedLocusNames=MT3082;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the conversion of 2 pyruvate molecules into
CC       acetolactate in the first common step of the biosynthetic pathway of
CC       the branched-amino acids such as leucine, isoleucine, and valine.
CC       {ECO:0000250}.
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; AE000516; AAK47411.1; -; Genomic_DNA.
DR   PIR; E70855; E70855.
DR   RefSeq; WP_003415167.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKJ2; -.
DR   SMR; P9WKJ2; -.
DR   EnsemblBacteria; AAK47411; AAK47411; MT3082.
DR   GeneID; 45426992; -.
DR   KEGG; mtc:MT3082; -.
DR   PATRIC; fig|83331.31.peg.3323; -.
DR   HOGENOM; CLU_055003_1_3_11; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000001020; 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   Gene3D; 3.30.70.1150; -; 1.
DR   InterPro; IPR004789; Acetalactate_synth_ssu.
DR   InterPro; IPR027271; Acetolactate_synth/TF_NikR_C.
DR   InterPro; IPR019455; Acetolactate_synth_ssu_C.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR039557; AHAS_ACT.
DR   PANTHER; PTHR30239; PTHR30239; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF10369; ALS_ss_C; 1.
DR   SUPFAM; SSF55021; SSF55021; 2.
DR   TIGRFAMs; TIGR00119; acolac_sm; 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..168
FT                   /note="Putative acetolactate synthase small subunit"
FT                   /id="PRO_0000427644"
FT   DOMAIN          7..82
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   168 AA;  18187 MW;  523488D6114AB354 CRC64;
     MSPKTHTLSV LVEDKPGVLA RVAALFSRRG FNIESLAVGA TECKDRSRMT IVVSAEDTPL
     EQITKQLNKL INVIKIVEQD DEHSVSRELA LIKVQADAGS RSQVIEAVNL FRANVIDVSP
     ESLTVEATGN RGKLEALLRV LEPFGIREIA QSGMVSLSRG PRGIGTAK