ID F4LQR7_TEPAE Unreviewed; 167 AA.
AC F4LQR7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:CDI40888.1};
GN OrderedLocusNames=TEPIRE1_2089 {ECO:0000313|EMBL:CDI40888.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CDI40888.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(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|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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HF563609; CDI40888.1; -; Genomic_DNA.
DR RefSeq; WP_013778992.1; NC_019954.2.
DR AlphaFoldDB; F4LQR7; -.
DR STRING; 1209989.TepRe1_1942; -.
DR KEGG; tae:TepiRe1_2089; -.
DR KEGG; tep:TepRe1_1942; -.
DR eggNOG; COG0440; Bacteria.
DR HOGENOM; CLU_055003_1_3_9; -.
DR OrthoDB; 9787365at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000010802; 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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000010802};
KW Transferase {ECO:0000256|RuleBase:RU368092, ECO:0000313|EMBL:CDI40888.1}.
FT DOMAIN 4..78
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 167 AA; 18503 MW; 4C25ECFCE6D49FC8 CRC64;
MKTTLSVLVE NQPGVLSRIA GLFSRRGFNI DSLAVGTTEN PDISRMTIVV EGDEYVVEQV
KKQLNKLVDV IKVSKIIPED SVTRELVLIK VDADSHMRSE IIQIAEIFRA SIVDVSQKSL
TIELTGDKDK IAAFEELLRP FGIKELVRTG VIAVNRGANT IKIEEEV
//
