ID   ILVH_MYCLE              Reviewed;         169 AA.
AC   O33113;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=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=ML1695;
GN   ORFNames=MLCB637.21;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; Z99263; CAB16436.1; -; Genomic_DNA.
DR   EMBL; AL583923; CAC30648.1; -; Genomic_DNA.
DR   PIR; T45414; T45414.
DR   RefSeq; NP_302165.1; NC_002677.1.
DR   RefSeq; WP_010908486.1; NC_002677.1.
DR   AlphaFoldDB; O33113; -.
DR   SMR; O33113; -.
DR   STRING; 272631.gene:17575540; -.
DR   KEGG; mle:ML1695; -.
DR   PATRIC; fig|272631.5.peg.3198; -.
DR   Leproma; ML1695; -.
DR   eggNOG; COG0440; Bacteria.
DR   HOGENOM; CLU_055003_1_3_11; -.
DR   OrthoDB; 9787365at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000000806; Chromosome.
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   Gene3D; 3.30.70.1150; ACT-like. Chain A, domain 2; 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   NCBIfam; TIGR00119; acolac_sm; 1.
DR   PANTHER; PTHR30239; ACETOLACTATE SYNTHASE SMALL SUBUNIT; 1.
DR   PANTHER; PTHR30239:SF0; ACETOLACTATE SYNTHASE SMALL SUBUNIT 1, CHLOROPLASTIC; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF10369; ALS_ss_C; 1.
DR   SUPFAM; SSF55021; ACT-like; 2.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..169
FT                   /note="Acetolactate synthase small subunit"
FT                   /id="PRO_0000151415"
FT   DOMAIN          8..85
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   169 AA;  18284 MW;  D450673379C88DD8 CRC64;
     MVGLPTHTLS VLVEDTPGVL ARVAALFSRR GFNIESLAVG ATECKTMSRM TIVVSAEETP
     LEQVTKQLHK LINVIKVVEQ EADNSLSREL ALIKVRAEAG TRSQVIEAVH LFRARVIDVS
     LESLTVEATG DCSKIEALLR VLEPFGVREI VQSGVVSLSR GPRGIGTVR
//