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Database: UniProt
Entry: Z9JZ30_9MICO
LinkDB: Z9JZ30_9MICO
Original site: Z9JZ30_9MICO 
ID   Z9JZ30_9MICO            Unreviewed;       177 AA.
AC   Z9JZ30;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
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   ORFNames=BF93_00425 {ECO:0000313|EMBL:EWS83066.1};
OS   Brachybacterium phenoliresistens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=396014 {ECO:0000313|EMBL:EWS83066.1, ECO:0000313|Proteomes:UP000023067};
RN   [1] {ECO:0000313|EMBL:EWS83066.1, ECO:0000313|Proteomes:UP000023067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W13A50 {ECO:0000313|EMBL:EWS83066.1,
RC   ECO:0000313|Proteomes:UP000023067};
RA   Wang X.;
RT   "Genome sequence of Brachybacterium phenoliresistens strain W13A50.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EWS83066.1}.
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DR   EMBL; JDYK01000001; EWS83066.1; -; Genomic_DNA.
DR   RefSeq; WP_051486339.1; NZ_KK069988.1.
DR   AlphaFoldDB; Z9JZ30; -.
DR   STRING; 396014.BF93_00425; -.
DR   PATRIC; fig|396014.3.peg.82; -.
DR   eggNOG; COG0440; Bacteria.
DR   HOGENOM; CLU_055003_1_3_11; -.
DR   OrthoDB; 9787365at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000023067; Unassembled WGS sequence.
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 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 {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   Reference proteome {ECO:0000313|Proteomes:UP000023067};
KW   Transferase {ECO:0000256|RuleBase:RU368092}.
FT   DOMAIN          13..87
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   177 AA;  19409 MW;  3606FF043AAAC471 CRC64;
     MDHSTTNPET TQTLSVLVEN KPGVLMRVSA LFARRGYNIA SLAVGPTEHP EISRITVVVD
     VAEHPLEQIT KQLNKLVNVL KIVQLEPRQS VQRELLLVKV RTDNTTRTSV LEIVQMFRAK
     VVDASPDAVT IEATGVDDKI TAMLSMLEPF GIREIVKSGA VAISRGGRSI TDRTLLS
//
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