ID U5Q7C9_9BACT Unreviewed; 172 AA.
AC U5Q7C9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:AGY53275.1};
GN ORFNames=BRDCF_p648 {ECO:0000313|EMBL:AGY53275.1};
OS Bacteroidales bacterium CF.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1400053 {ECO:0000313|EMBL:AGY53275.1, ECO:0000313|Proteomes:UP000017642};
RN [1] {ECO:0000313|EMBL:AGY53275.1, ECO:0000313|Proteomes:UP000017642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AGY53275.1};
RX PubMed=24356833;
RA Tang S., Edwards E.A.;
RT "Complete Genome Sequence of Bacteroidales Strain CF from a Chloroform-
RT Dechlorinating Enrichment Culture.";
RL Genome Announc. 1:e01066-13(2013).
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|RuleBase:RU368092}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {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|RuleBase:RU368092}.
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DR EMBL; CP006772; AGY53275.1; -; Genomic_DNA.
DR AlphaFoldDB; U5Q7C9; -.
DR STRING; 1400053.BRDCF_p648; -.
DR KEGG; bacc:BRDCF_p648; -.
DR HOGENOM; CLU_055003_3_1_10; -.
DR OrthoDB; 1523722at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000017642; Chromosome.
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 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 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; 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|RuleBase:RU368092};
KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU368092};
KW Reference proteome {ECO:0000313|Proteomes:UP000017642};
KW Transferase {ECO:0000256|RuleBase:RU368092, ECO:0000313|EMBL:AGY53275.1}.
FT DOMAIN 6..80
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 172 AA; 19648 MW; 6AA8E8F22B4BA1F6 CRC64;
MEREYIVVAN VNNQISVLNR ITSVYLKRHI NIESLNVSES YIKGISTVVI SAITSTNITQ
KIVNQLDNII DVYSVDFYLP EDIIYKELAL YKVDSRILSD KRESAFLLNE SHGRIMEISK
DYVVIEKSGT RGELEKLRDR LDIKGLLAGY SRSGNVVLHR EENITNILQK VS
//
