ID B1LKZ7_ECOSM Unreviewed; 96 AA.
AC B1LKZ7;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN Name=ilvN {ECO:0000313|EMBL:ACB20204.1};
GN OrderedLocusNames=EcSMS35_4037 {ECO:0000313|EMBL:ACB20204.1};
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB20204.1, ECO:0000313|Proteomes:UP000007011};
RN [1] {ECO:0000313|EMBL:ACB20204.1, ECO:0000313|Proteomes:UP000007011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX PubMed=18708504; DOI=10.1128/JB.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
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 -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC -!- SUBUNIT: Dimer of large and small chains.
CC {ECO:0000256|ARBA:ARBA00011744}.
CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000256|ARBA:ARBA00006341}.
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DR EMBL; CP000970; ACB20204.1; -; Genomic_DNA.
DR RefSeq; WP_001181706.1; NC_010498.1.
DR AlphaFoldDB; B1LKZ7; -.
DR SMR; B1LKZ7; -.
DR GeneID; 75205384; -.
DR KEGG; ecm:EcSMS35_4037; -.
DR HOGENOM; CLU_165363_0_0_6; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000007011; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04878; ACT_AHAS; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR InterPro; IPR004789; Acetalactate_synth_ssu.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR039557; AHAS_ACT.
DR PANTHER; PTHR30239:SF4; ACETOLACTATE SYNTHASE ISOZYME 1 SMALL SUBUNIT; 1.
DR PANTHER; PTHR30239; ACETOLACTATE SYNTHASE SMALL SUBUNIT; 1.
DR Pfam; PF01842; ACT; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR PROSITE; PS51671; ACT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Transferase {ECO:0000313|EMBL:ACB20204.1}.
FT DOMAIN 10..83
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 55..82
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 96 AA; 11106 MW; 7F37DD421EDD3802 CRC64;
MQNTTHDNVI LELTVRNHPG VMTHVCGLFA RRAFNVEGIL CLPIQDSDKS HIWLLVNDDQ
RLEQMISQID KLEDVVKVQR NQSDPTMFNK IAVFFQ
//
