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Protein

Acetolactate synthase isozyme 2 large subunit

Gene

ilvG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first step in the biosynthesis of branched-chain amino acids.

Catalytic activityi

2 pyruvate = 2-acetolactate + CO2.

Cofactori

Protein has several cofactor binding sites:
  • FAD1 PublicationNote: Binds 1 FAD per subunit. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry. However, after removal of the FAD no AHAS activity can be detected (PubMed:9581571), indicating that the cofactor is essential. The large subunit alone does not bind FAD, and FAD is not necessary for association of the subunits.1 Publication
  • Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit. Is not necessary for subunit association.1 Publication
  • thiamine diphosphate1 PublicationNote: Binds 1 thiamine pyrophosphate per subunit. Is not necessary for subunit association.1 Publication

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471Thiamine pyrophosphateBy similarity
Binding sitei149 – 1491FADBy similarity
Metal bindingi428 – 4281MagnesiumBy similarity
Metal bindingi455 – 4551MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi251 – 27222FADBy similarityAdd
BLAST
Nucleotide bindingi294 – 31320FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciEcoCyc:G8221-MONOMER.
EcoCyc:LARGEILVG-MONOMER.
MetaCyc:G8221-MONOMER.
MetaCyc:LARGEILVG-MONOMER.
SABIO-RKP00892.
UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetolactate synthase isozyme 2 large subunit (EC:2.2.1.6)
Short name:
AHAS-II
Alternative name(s):
ALS-II
Acetohydroxy-acid synthase II large subunit
Gene namesi
Name:ilvG
Ordered Locus Names:b4488
ORF Names:b3767
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10498. ilvG.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Acetolactate synthase isozyme 2 large subunitPRO_0000090788Add
BLAST

Interactioni

Subunit structurei

Tetramer of two large (IlvG) and two small (IlvM) chains.1 Publication

Protein-protein interaction databases

DIPiDIP-10023N.
IntActiP00892. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP00892.
SMRiP00892. Positions 3-544.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni377 – 45781Thiamine pyrophosphate bindingAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

HOGENOMiHOG000258448.
InParanoidiP00892.
OMAiHSWVVRD.
PhylomeDBiP00892.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012846. Acetolactate_synth_lsu.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00118. acolac_lg. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00892-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGAQWVVHA LRAQGVNTVF GYPGGAIMPV YDALYDGGVE HLLCRHEQGA
60 70 80 90 100
AMAAIGYARA TGKTGVCIAT SGPGATNLIT GLADALLDSI PVVAITGQVS
110 120 130 140 150
APFIGTDAFQ EVDVLGLSLA CTKHSFLVQS LEELPRIMAE AFDVACSGRP
160 170 180 190 200
GPVLVDIPKD IQLASGDLEP WFTTVENEVT FPHAEVEQAR QMLAKAQKPM
210 220 230 240 250
LYVGGGVGMA QAVPALREFL AATKMPATCT LKGLGAVEAD YPYYLGMLGM
260 270 280 290 300
HGTKAANFAV QECDLLIAVG ARFDDRVTGK LNTFAPHASV IHMDIDPAEM
310 320 330 340 350
NKLRQAHVAL QGDLNALLPA LQQPLNQYDW QQHCAQLRDE HSWRYDHPGD
360 370 380 390 400
AIYAPLLLKQ LSDRKPADCV VTTDVGQHQM WAAQHIAHTR PENFITSSGL
410 420 430 440 450
GTMGFGLPAA VGAQVARPND TVVCISGDGS FMMNVQELGT VKRKQLPLKI
460 470 480 490 500
VLLDNQRLGM VRQWQQLFFQ ERYSETTLTD NPDFLMLASA FGIHGQHITR
510 520 530 540
KDQVEAALDT MLNSDGPYLL HVSIDELENV WPLVPPGASN SEMLEKLS
Length:548
Mass (Da):59,285
Last modified:July 19, 2003 - v3
Checksum:iA002C07DAA6476DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti284 – 2841F → S in AAA24021 (PubMed:3550695).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32253 Genomic DNA. Translation: AAA24021.1.
X04890 Genomic DNA. Translation: CAA28573.1.
M87049 Genomic DNA. Translation: AAA67571.1. Sequence problems.
U00096 Genomic DNA. No translation available.
M37337 Genomic DNA. Translation: AAA24608.1.
V00289 Genomic DNA. Translation: CAA23556.1.
M10313 Genomic DNA. Translation: AAB59050.1.
V00290 Genomic DNA. Translation: CAA23558.1. Sequence problems.
X02413 Genomic DNA. Translation: CAA26260.1.
PIRiA26570. YCEC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32253 Genomic DNA. Translation: AAA24021.1.
X04890 Genomic DNA. Translation: CAA28573.1.
M87049 Genomic DNA. Translation: AAA67571.1. Sequence problems.
U00096 Genomic DNA. No translation available.
M37337 Genomic DNA. Translation: AAA24608.1.
V00289 Genomic DNA. Translation: CAA23556.1.
M10313 Genomic DNA. Translation: AAB59050.1.
V00290 Genomic DNA. Translation: CAA23558.1. Sequence problems.
X02413 Genomic DNA. Translation: CAA26260.1.
PIRiA26570. YCEC.

3D structure databases

ProteinModelPortaliP00892.
SMRiP00892. Positions 3-544.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10023N.
IntActiP00892. 2 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

EchoBASEiEB0493.
EcoGeneiEG10498. ilvG.

Phylogenomic databases

HOGENOMiHOG000258448.
InParanoidiP00892.
OMAiHSWVVRD.
PhylomeDBiP00892.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.
BioCyciEcoCyc:G8221-MONOMER.
EcoCyc:LARGEILVG-MONOMER.
MetaCyc:G8221-MONOMER.
MetaCyc:LARGEILVG-MONOMER.
SABIO-RKP00892.

Miscellaneous databases

PROiP00892.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012846. Acetolactate_synth_lsu.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00118. acolac_lg. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete nucleotide sequence of the ilvGMEDA operon of Escherichia coli K-12."
    Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E., Hatfield G.W.
    Nucleic Acids Res. 15:2137-2155(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
    Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
    Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Sequence and transcriptional activity of the Escherichia coli K-12 chromosome region between rrnC and ilvGMEDA."
    Coppola G., Huang F., Riley J., Cox J.L., Hantzopoulos P., Zhou L.-B., Calhoun D.H.
    Gene 97:21-27(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-402.
    Strain: K12.
  5. "Multivalent translational control of transcription termination at attenuator of ilvGEDA operon of Escherichia coli K-12."
    Lawther R.P., Hatfield G.W.
    Proc. Natl. Acad. Sci. U.S.A. 77:1862-1866(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
    Strain: K12.
  6. "Purification of Escherichia coli acetohydroxyacid synthase isoenzyme II and reconstitution of active enzyme from its individual pure subunits."
    Hill C.M., Pang S.S., Duggleby R.G.
    Biochem. J. 327:891-898(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-3, SUBUNIT, COFACTOR, REMOVAL OF FAD COFACTOR.
    Strain: K12 / mutant ILV02096.
  7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-548, IDENTIFICATION OF FRAMESHIFT THAT RESTORES THE READING FRAME.
    Strain: K12 / mutant ILV02096.
  8. "Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence."
    Kuramitsu S., Ogawa T., Ogawa H., Kagamiyama H.
    J. Biochem. 97:993-999(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 543-548.
    Strain: K12.

Entry informationi

Entry nameiILVG_ECOLI
AccessioniPrimary (citable) accession number: P00892
Secondary accession number(s): P76749
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 19, 2003
Last modified: November 11, 2015
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

E.coli contains genes for 3 AHAS isozymes: ilvBN, ilvGM and ilvIH. In strain K12 only the Val-inhibitable ilvBN and ilvIH are expressed; ilvGM has a defect that disturbs the ilvG reading frame. IlvG (this protein) is Val-resistant and is expressed in K12 strains having what used to be referred to as ilv0 mutations. The ilv02096 mutation (shown here, an insertion of 2 bp, PubMed:7015336) causes a frameshift which restores the open reading frame, permitting the expression of this isozyme.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.