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Database: UniProt
Entry: C1DFH8_AZOVD
LinkDB: C1DFH8_AZOVD
Original site: C1DFH8_AZOVD 
ID   C1DFH8_AZOVD            Unreviewed;       163 AA.
AC   C1DFH8;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   13-SEP-2023, entry version 66.
DE   RecName: Full=Acetolactate synthase small subunit {ECO:0000256|RuleBase:RU368092};
DE            Short=AHAS {ECO:0000256|RuleBase:RU368092};
DE            Short=ALS {ECO:0000256|RuleBase:RU368092};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU368092};
DE   AltName: Full=Acetohydroxy-acid synthase small subunit {ECO:0000256|RuleBase:RU368092};
GN   Name=ilvH {ECO:0000313|EMBL:ACO80374.1};
GN   OrderedLocusNames=Avin_42510 {ECO:0000313|EMBL:ACO80374.1};
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO80374.1, ECO:0000313|Proteomes:UP000002424};
RN   [1] {ECO:0000313|EMBL:ACO80374.1, ECO:0000313|Proteomes:UP000002424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX   PubMed=19429624; DOI=10.1128/JB.00504-09;
RA   Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
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:0000256|RuleBase:RU368092}.
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         Evidence={ECO:0000256|ARBA:ARBA00000673,
CC         ECO:0000256|RuleBase:RU368092};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU368092}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC       ECO:0000256|RuleBase:RU368092}.
CC   -!- SUBUNIT: Dimer of large and small chains.
CC       {ECO:0000256|ARBA:ARBA00011744, ECO:0000256|RuleBase:RU368092}.
CC   -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC       {ECO:0000256|ARBA:ARBA00006341, ECO:0000256|RuleBase:RU368092}.
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DR   EMBL; CP001157; ACO80374.1; -; Genomic_DNA.
DR   RefSeq; WP_012702742.1; NC_012560.1.
DR   AlphaFoldDB; C1DFH8; -.
DR   STRING; 322710.Avin_42510; -.
DR   EnsemblBacteria; ACO80374; ACO80374; Avin_42510.
DR   KEGG; avn:Avin_42510; -.
DR   eggNOG; COG0440; Bacteria.
DR   HOGENOM; CLU_055003_1_3_6; -.
DR   OMA; MLEPFGI; -.
DR   OrthoDB; 9787365at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000002424; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
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 2, CHLOROPLASTIC; 1.
DR   Pfam; PF13710; ACT_5; 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 {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU368092};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|RuleBase:RU368092};
KW   Transferase {ECO:0000256|RuleBase:RU368092}.
FT   DOMAIN          4..78
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   163 AA;  17883 MW;  FC7A5073086BE468 CRC64;
     MRHIISLLLE NEPGALSRVV GLFSQRNYNI ETLTVAPTED PTLSRLTLTT IGQDEVIEQI
     TKNLNKLIEV VKLVDLSESA HIERELLLVK VKATGAQRAE IKRTTDIFRG QIVDVTSSVY
     TIQLTGTSDK LDSFLHAIGT SSILETVRSG VTGIARGDKV LTI
//
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