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Entry version 14 (22 Apr 2020)
Sequence version 1 (27 Sep 2017)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the first step in the biosynthesis of branched-chain amino acids.1 Publication

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 frameshift 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. The inactive N-terminal pseudogene fragment is found here (AC P0DP89).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by the herbicides chlorimuron ethyl, chlorsulfuron and imazapyr.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=2.6 mM for pyruvate1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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), Putative acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase (ilvB), Acetolactate synthase (FAZ83_14160), Acetolactate synthase (ilvI), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase (ilvN), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase (ilvN)
    2. Ketol-acid reductoisomerase (NADP(+)) (ilvC), Ketol-acid reductoisomerase (NADP(+)) (ilvC)
    3. Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD)
    4. Branched-chain-amino-acid aminotransferase (ilvE), 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.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei47Thiamine pyrophosphateBy similarity1
    Binding sitei149FADBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi428MagnesiumBy similarity1
    Metal bindingi455MagnesiumBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi251 – 272FADBy similarityAdd BLAST22
    Nucleotide bindingi294 – 313FADBy similarityAdd BLAST20

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionTransferase
    Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
    LigandFAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

    Enzyme and pathway databases

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00047;UER00055
    UPA00049;UER00059

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Acetolactate synthase isozyme 2 large subunit (EC:2.2.1.61 Publication)
    Short name:
    AHAS-II
    Alternative name(s):
    ALS-II
    Acetohydroxy-acid synthase II large subunit
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:ilvG
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000907881 – 548Acetolactate synthase isozyme 2 large subunitAdd BLAST548

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

    1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-3570, Acetolactate synthase II complex

    Protein interaction database and analysis system

    More...
    IntActi
    P0DP90, 4 interactors

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P0DP90

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni377 – 457Thiamine pyrophosphate bindingAdd BLAST81

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the TPP enzyme family.Curated

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd02015, TPP_AHAS, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR012846, Acetolactate_synth_lsu
    IPR039368, AHAS_TPP
    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

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02775, TPP_enzyme_C, 1 hit
    PF00205, TPP_enzyme_M, 1 hit
    PF02776, TPP_enzyme_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52467, SSF52467, 1 hit
    SSF52518, SSF52518, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00118, acolac_lg, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00187, TPP_ENZYMES, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P0DP90-1 [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:September 27, 2017 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA002C07DAA6476DA
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti284F → S in AAA24021 (PubMed:3550695).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    M32253 Genomic DNA Translation: AAA24021.1
    X04890 Genomic DNA Translation: CAA28573.1
    M37337 Genomic DNA Translation: AAA24608.1
    V00289 Genomic DNA Translation: CAA23556.1
    M10313 Genomic DNA Translation: AAB59050.1
    X02413 Genomic DNA Translation: CAA26260.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A26570, YCEC

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
    M37337 Genomic DNA Translation: AAA24608.1
    V00289 Genomic DNA Translation: CAA23556.1
    M10313 Genomic DNA Translation: AAB59050.1
    X02413 Genomic DNA Translation: CAA26260.1
    PIRiA26570, YCEC

    3D structure databases

    SMRiP0DP90
    ModBaseiSearch...

    Protein-protein interaction databases

    ComplexPortaliCPX-3570, Acetolactate synthase II complex
    IntActiP0DP90, 4 interactors

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0493

    Enzyme and pathway databases

    UniPathwayiUPA00047;UER00055
    UPA00049;UER00059

    Family and domain databases

    CDDicd02015, TPP_AHAS, 1 hit
    InterProiView protein in InterPro
    IPR012846, Acetolactate_synth_lsu
    IPR039368, AHAS_TPP
    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
    PfamiView protein in Pfam
    PF02775, TPP_enzyme_C, 1 hit
    PF00205, TPP_enzyme_M, 1 hit
    PF02776, TPP_enzyme_N, 1 hit
    SUPFAMiSSF52467, SSF52467, 1 hit
    SSF52518, SSF52518, 2 hits
    TIGRFAMsiTIGR00118, acolac_lg, 1 hit
    PROSITEiView protein in PROSITE
    PS00187, TPP_ENZYMES, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiILVG_ECOLI
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0DP90
    Secondary accession number(s): P00892, P76749
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2017
    Last sequence update: September 27, 2017
    Last modified: April 22, 2020
    This is version 14 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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