ID   ILVH_BACSU              Reviewed;         172 AA.
AC   P37252;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   03-AUG-2022, entry version 135.
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=BSU28300;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Vandeyar M.A., Vander Horn P.B., Rafael J.A., Grandoni J.A., Zahler S.A.;
RT   "The ilv-leu operon of Bacillus subtilis: sequences of the ilvB, ilvN and
RT   ilvC genes, and the control of transcription.";
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO C-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
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; L03181; AAA22547.1; -; Genomic_DNA.
DR   EMBL; Z75208; CAA99562.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14790.2; -; Genomic_DNA.
DR   PIR; E69644; E69644.
DR   RefSeq; NP_390708.2; NC_000964.3.
DR   RefSeq; WP_004399096.1; NZ_JNCM01000036.1.
DR   RefSeq; WP_009967931.1; NZ_CM000487.1.
DR   AlphaFoldDB; P37252; -.
DR   SMR; P37252; -.
DR   STRING; 224308.BSU28300; -.
DR   PaxDb; P37252; -.
DR   PRIDE; P37252; -.
DR   EnsemblBacteria; CAB14790; CAB14790; BSU_28300.
DR   GeneID; 937477; -.
DR   KEGG; bsu:BSU28300; -.
DR   PATRIC; fig|224308.179.peg.3074; -.
DR   eggNOG; COG0440; Bacteria.
DR   InParanoid; P37252; -.
DR   OMA; EPYGIKE; -.
DR   PhylomeDB; P37252; -.
DR   BioCyc; BSUB:BSU28300-MON; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR   GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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   Reference proteome; Transferase.
FT   CHAIN           1..172
FT                   /note="Acetolactate synthase small subunit"
FT                   /id="PRO_0000151406"
FT   DOMAIN          4..79
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   CONFLICT        160..172
FT                   /note="QQKASSNKTISIV -> SKRRHPIKQYLLYKT (in Ref. 1;
FT                   AAA22547 and 2; CAA99562)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   172 AA;  18925 MW;  AB4180EC8D3EA29A CRC64;
     MKRIITLTVV NRSGVLNRIT GLFTKRHYNI ESITVGHTET AGVSRITFVV HVEGENDVEQ
     LTKQLNKQID VLKVTDITNQ SIVQRELALI KVVSAPSTRT EINGIIEPFR ASVVDVSRDS
     IVVQVTGESN KIEALIELLK PYGIKEIART GTTAFARGTQ QKASSNKTIS IV