ID D1J7C0_ECTSI Unreviewed; 194 AA.
AC D1J7C0;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
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:CAV31304.1};
GN ORFNames=Es_cpDNA_162 {ECO:0000313|EMBL:CAV31304.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OG Plastid; Chloroplast {ECO:0000313|EMBL:CAV31304.1}.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CAV31304.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAV31304.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=19835607; DOI=10.1186/1471-2148-9-253;
RA Le Corguille G., Pearson G., Valente M., Viegas C., Gschloessl B.,
RA Corre E., Bailly X., Peters A.F., Jubin C., Vacherie B., Cock J.M.,
RA Leblanc C.;
RT "Plastid genomes of two brown algae, Ectocarpus siliculosus and Fucus
RT vesiculosus: further insights on the evolution of red-algal derived
RT plastids.";
RL BMC Evol. Biol. 9:253-253(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|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|RuleBase:RU368092}.
CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000256|RuleBase:RU368092}.
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DR EMBL; FP102343; CAT18856.1; -; Genomic_DNA.
DR EMBL; FP102296; CAV31304.1; -; Genomic_DNA.
DR RefSeq; YP_003289273.1; NC_013498.1.
DR AlphaFoldDB; D1J7C0; -.
DR STRING; 2880.D1J7C0; -.
DR GeneID; 8594791; -.
DR eggNOG; KOG2663; Eukaryota.
DR InParanoid; D1J7C0; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000002630; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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; 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|RuleBase:RU368092};
KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU368092};
KW Chloroplast {ECO:0000313|EMBL:CAV31304.1};
KW Plastid {ECO:0000313|EMBL:CAV31304.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Transferase {ECO:0000256|RuleBase:RU368092, ECO:0000313|EMBL:CAV31304.1}.
FT DOMAIN 4..81
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 194 AA; 22292 MW; 0131C9D4F36DE385 CRC64;
MERTISVLVE KDPGGLVRII SLLTRRRFHI KSITLSPCER KGYERIIIVV INQSDGVDAG
KQLTKQIRKL INVVNVQDIT YLPLIERELV LIKLKVNLIE RTEILNLAQI FRFKITDVTD
STLILEVTAD PGKIAALEKV LEKYNILQLV RTGRIALIRE SRVSTSSLKE YPEFEVLTGQ
NYLNNIEDLF KKDY
//
