ILVGP_ECOLI
ID ILVGP_ECOLI Reviewed; 327 AA.
AC P0DP89; 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=Putative acetolactate synthase isozyme 2 large subunit;
DE Short=AHAS-II;
DE AltName: Full=ALS-II;
DE AltName: Full=Acetohydroxy-acid synthase II large subunit;
GN Name=ilvG; OrderedLocusNames=b4488; ORFNames=b3767;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-327, AND IDENTIFICATION OF
RP FRAMESHIFT THAT RESTORES THE READING FRAME.
RC STRAIN=K12;
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).
CC -!- FUNCTION: N-terminal pseudogene fragment of this gene. If the reading
CC frame is restored, catalyzes the first step in the biosynthesis of
CC branched-chain amino acids. {ECO:0000250|UniProtKB:P0DP90,
CC ECO:0000305|PubMed:7015336}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P0DP90};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P0DP90};
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:0000250|UniProtKB:P0DP90}.
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 The ilv02096 mutation causes another frameshift which restores the open
CC reading frame, permitting the expression of this isozyme and can be
CC seen in entry (AC P0DP90). Restored IlvG is Val-resistant and is
CC expressed in K12 strains having what used to be referred to as ilv0
CC mutations. {ECO:0000305|PubMed:7015336}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. A frameshift removes the
CC C-terminus. A full-length restored gene can be seen in (AC P0DP90).
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23558.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M87049; AAA67571.1; -; Genomic_DNA.
DR EMBL; U00096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; V00290; CAA23558.1; ALT_INIT; Genomic_DNA.
DR PIR; A26570; YCEC.
DR AlphaFoldDB; P0DP89; -.
DR SMR; P0DP89; -.
DR EchoBASE; EB0493; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR PRO; PR:P0DP89; -.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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; IPR045229; TPP_enz.
DR PANTHER; PTHR18968; PTHR18968; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
PE 5: Uncertain;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; FAD;
KW Flavoprotein; Reference proteome.
FT CHAIN 1..327
FT /note="Putative acetolactate synthase isozyme 2 large
FT subunit"
FT /id="PRO_0000441723"
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"
SQ SEQUENCE 327 AA; 34507 MW; AB0141C73BDA2AF0 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 LQQPLNQ
