ILVG_ECOLI
ID ILVG_ECOLI Reviewed; 548 AA.
AC P0DP90; P00892; P76749;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Acetolactate synthase isozyme 2 large subunit;
DE Short=AHAS-II;
DE EC=2.2.1.6 {ECO:0000269|PubMed:9581571};
DE AltName: Full=ALS-II;
DE AltName: Full=Acetohydroxy-acid synthase II large subunit;
GN Name=ilvG;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / mutant ILV02096;
RX PubMed=3550695; DOI=10.1093/nar/15.5.2137;
RA Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E.,
RA Hatfield G.W.;
RT "The complete nucleotide sequence of the ilvGMEDA operon of Escherichia
RT coli K-12.";
RL Nucleic Acids Res. 15:2137-2155(1987).
RN [2]
RP ERRATUM OF PUBMED:3550695.
RA Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E.,
RA Hatfield G.W.;
RL Nucleic Acids Res. 15:9108-9108(1987).
RN [3]
RP ERRATUM OF PUBMED:3550695.
RA Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E.,
RA Hatfield G.W.;
RL Nucleic Acids Res. 16:3602-3602(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-402.
RC STRAIN=K12;
RX PubMed=1995430; DOI=10.1016/0378-1119(91)90005-v;
RA Coppola G., Huang F., Riley J., Cox J.L., Hantzopoulos P., Zhou L.-B.,
RA Calhoun D.H.;
RT "Sequence and transcriptional activity of the Escherichia coli K-12
RT chromosome region between rrnC and ilvGMEDA.";
RL Gene 97:21-27(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RC STRAIN=K12;
RX PubMed=6154938; DOI=10.1073/pnas.77.4.1862;
RA Lawther R.P., Hatfield G.W.;
RT "Multivalent translational control of transcription termination at
RT attenuator of ilvGEDA operon of Escherichia coli K-12.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:1862-1866(1980).
RN [6]
RP PROTEIN SEQUENCE OF 1-3, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, REMOVAL OF
RP FAD COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=K12 / mutant ILV02096;
RX PubMed=9581571; DOI=10.1042/bj3270891;
RA Hill C.M., Pang S.S., Duggleby R.G.;
RT "Purification of Escherichia coli acetohydroxyacid synthase isoenzyme II
RT and reconstitution of active enzyme from its individual pure subunits.";
RL Biochem. J. 327:891-898(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-548, AND IDENTIFICATION OF
RP FRAMESHIFT THAT RESTORES THE READING FRAME.
RC STRAIN=K12 / mutant ILV02096;
RX PubMed=7015336; DOI=10.1073/pnas.78.2.922;
RA Lawther R.P., Calhoun D.H., Adams C.W., Hauser C.A., Gray J.,
RA Hatfield G.W.;
RT "Molecular basis of valine resistance in Escherichia coli K-12.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:922-925(1981).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 543-548.
RC STRAIN=K12;
RX PubMed=3897211; DOI=10.1093/oxfordjournals.jbchem.a135176;
RA Kuramitsu S., Ogawa T., Ogawa H., Kagamiyama H.;
RT "Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide
RT sequence of the ilvE gene and the deduced amino acid sequence.";
RL J. Biochem. 97:993-999(1985).
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of branched-
CC chain amino acids. {ECO:0000269|PubMed:9581571}.
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:0000269|PubMed:9581571};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:9581571};
CC Note=Binds 1 FAD per subunit. The role of this cofactor is not clear
CC considering that the reaction does not involve redox chemistry.
CC However, after removal of the FAD no AHAS activity can be detected
CC (PubMed:9581571), indicating that the cofactor is essential. The large
CC subunit alone does not bind FAD, and FAD is not necessary for
CC association of the subunits. {ECO:0000269|PubMed:9581571};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9581571};
CC Note=Binds 1 Mg(2+) ion per subunit. Is not necessary for subunit
CC association. {ECO:0000269|PubMed:9581571};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:9581571};
CC Note=Binds 1 thiamine pyrophosphate per subunit. Is not necessary for
CC subunit association. {ECO:0000269|PubMed:9581571};
CC -!- ACTIVITY REGULATION: Inhibited by the herbicides chlorimuron ethyl,
CC chlorsulfuron and imazapyr. {ECO:0000269|PubMed:9581571}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 mM for pyruvate {ECO:0000269|PubMed:9581571};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4.
CC -!- SUBUNIT: Tetramer of two large (IlvG) and two small (IlvM) chains.
CC {ECO:0000269|PubMed:9581571}.
CC -!- INTERACTION:
CC P0DP90; P0ADG1: ilvM; NbExp=2; IntAct=EBI-1133701, EBI-1133722;
CC -!- MISCELLANEOUS: E.coli contains genes for 3 AHAS isozymes: ilvBN, ilvGM
CC and ilvIH. In strain K12 only the Val-inhibitable ilvBN and ilvIH are
CC expressed; ilvGM has a frameshift that disturbs the ilvG reading frame.
CC IlvG (this protein) is Val-resistant and is expressed in K12 strains
CC having what used to be referred to as ilv0 mutations. The ilv02096
CC mutation (shown here, an insertion of 2 bp, PubMed:7015336) causes a
CC frameshift which restores the open reading frame, permitting the
CC expression of this isozyme. The inactive N-terminal pseudogene fragment
CC is found here (AC P0DP89). {ECO:0000269|PubMed:7015336}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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; M32253; AAA24021.1; -; Genomic_DNA.
DR EMBL; X04890; CAA28573.1; -; Genomic_DNA.
DR EMBL; M37337; AAA24608.1; -; Genomic_DNA.
DR EMBL; V00289; CAA23556.1; -; Genomic_DNA.
DR EMBL; M10313; AAB59050.1; -; Genomic_DNA.
DR EMBL; X02413; CAA26260.1; -; Genomic_DNA.
DR PIR; A26570; YCEC.
DR AlphaFoldDB; P0DP90; -.
DR SMR; P0DP90; -.
DR ComplexPortal; CPX-3570; Acetolactate synthase II complex.
DR IntAct; P0DP90; 4.
DR EchoBASE; EB0493; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR GO; GO:0005948; C:acetolactate synthase complex; IPI:ComplexPortal.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02015; TPP_AHAS; 1.
DR InterPro; IPR012846; Acetolactate_synth_lsu.
DR InterPro; IPR039368; AHAS_TPP.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00118; acolac_lg; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Direct protein sequencing; FAD; Flavoprotein; Magnesium; Metal-binding;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..548
FT /note="Acetolactate synthase isozyme 2 large subunit"
FT /id="PRO_0000090788"
FT REGION 377..457
FT /note="Thiamine pyrophosphate binding"
FT BINDING 47
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 251..272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 294..313
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 284
FT /note="F -> S (in Ref. 1; AAA24021)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 59285 MW; A002C07DAA6476DA CRC64;
MNGAQWVVHA LRAQGVNTVF GYPGGAIMPV YDALYDGGVE HLLCRHEQGA AMAAIGYARA
TGKTGVCIAT SGPGATNLIT GLADALLDSI PVVAITGQVS APFIGTDAFQ EVDVLGLSLA
CTKHSFLVQS LEELPRIMAE AFDVACSGRP GPVLVDIPKD IQLASGDLEP WFTTVENEVT
FPHAEVEQAR QMLAKAQKPM LYVGGGVGMA QAVPALREFL AATKMPATCT LKGLGAVEAD
YPYYLGMLGM HGTKAANFAV QECDLLIAVG ARFDDRVTGK LNTFAPHASV IHMDIDPAEM
NKLRQAHVAL QGDLNALLPA LQQPLNQYDW QQHCAQLRDE HSWRYDHPGD AIYAPLLLKQ
LSDRKPADCV VTTDVGQHQM WAAQHIAHTR PENFITSSGL GTMGFGLPAA VGAQVARPND
TVVCISGDGS FMMNVQELGT VKRKQLPLKI VLLDNQRLGM VRQWQQLFFQ ERYSETTLTD
NPDFLMLASA FGIHGQHITR KDQVEAALDT MLNSDGPYLL HVSIDELENV WPLVPPGASN
SEMLEKLS
