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Protein

Glutathione hydrolase proenzyme

Gene

ggt

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

Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D-gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acceptors (PubMed:2877974). The KM values for gamma-glutamyl acceptors are so high that it has been proposed transpeptidation is not the physiological role in E.coli (PubMed:2877974, PubMed:8104180).1 Publication1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 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

Transferase and hydrolase activities are inhibited by L-Ala and L-Gln, and also by GGT affinity labeling reagents such as azaserine and 6-diazo-5-oxo-nor-leucine.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=35 µM for glutathione transfer to glycylglycine (gly-gly)1 Publication
  2. KM=35 µM for gamma-glutamyl-p-nitroanilide (gamma-GpNA) transfer to gly-gly1 Publication
  3. KM=29 µM for glutathione hydrolysis1 Publication
  4. KM=68 µM for gamma-GpNA hydrolysis1 Publication

    pH dependencei

    Optimum pH is 8.73 for transfer of p-nitroanilide from gamma-GpNA to gly-gly and 9.25 for hydrolysis of gamma-GpNA.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius for both transferase and hydrolase activities.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glutathione metabolism

    This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.
    View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei114Glutamate1 Publication1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei391Nucleophile2 Publications1
    Binding sitei409Glutamate1 Publication1
    Binding sitei411Glutamate1 Publication1
    Binding sitei430Glutamate1 Publication1
    Binding sitei433Glutamate1 Publication1

    <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

    • amino acid salvage Source: EcoCyc
    • glutathione biosynthetic process Source: UniProtKB-KW
    • glutathione catabolic process Source: InterPro
    • self proteolysis Source: EcoCyc

    <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 functionAcyltransferase, Hydrolase, Protease, Transferase
    Biological processGlutathione biosynthesis

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:EG10374-MONOMER
    MetaCyc:EG10374-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.3.2.2 2026
    3.4.19.13 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P18956

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

    More...
    UniPathwayi
    UPA00204

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    T03.001

    <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_and_taxonomy_section">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:
    Glutathione hydrolase proenzyme (EC:3.4.19.131 Publication)
    Alternative name(s):
    Gamma-glutamyltranspeptidase proenzyme1 Publication (EC:2.3.2.21 Publication)
    Short name:
    GGT
    Cleaved into the following 2 chains:
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:ggt
    Ordered Locus Names:b3447, JW3412
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG10374 ggt

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Periplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Loss of growth using exogenous gamma-glutamyl peptides as amino acid sources.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi391T → A: Abolishes autocatalytic cleavage, loss of enzymatic activity. 1 Publication1
    Mutagenesisi513R → A: Not processed into its subunits, loss of enzymatic activity. 1 Publication1
    Mutagenesisi571R → G: Not processed into its subunits, loss of enzymatic activity. 1 Publication1

    <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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 251 PublicationAdd BLAST25
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001105226 – 390Glutathione hydrolase large chainAdd BLAST365
    ChainiPRO_0000011053391 – 580Glutathione hydrolase small chainAdd BLAST190

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Cleaved by autocatalysis into a large and a small subunit.5 Publications

    Keywords - PTMi

    Zymogen

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P18956

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P18956

    <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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.5 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4261666, 434 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-9758N

    Protein interaction database and analysis system

    More...
    IntActi
    P18956, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_3621

    <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

    Secondary structure

    1580
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P18956

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

    More...
    SMRi
    P18956

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P18956

    <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>Regioni462 – 463Glutamate binding2
    Regioni483 – 484Glutamate binding2

    <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 gamma-glutamyltransferase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CFB Bacteria
    COG0405 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000175617

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P18956

    KEGG Orthology (KO)

    More...
    KOi
    K00681

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P18956

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000101 GGT_peptidase
    IPR029055 Ntn_hydrolases_N

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56235 SSF56235, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00066 g_glut_trans, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00462 G_GLU_TRANSPEPTIDASE, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P18956-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MIKPTFLRRV AIAALLSGSC FSAAAAPPAP PVSYGVEEDV FHPVRAKQGM
    60 70 80 90 100
    VASVDATATQ VGVDILKEGG NAVDAAVAVG YALAVTHPQA GNLGGGGFML
    110 120 130 140 150
    IRSKNGNTTA IDFREMAPAK ATRDMFLDDQ GNPDSKKSLT SHLASGTPGT
    160 170 180 190 200
    VAGFSLALDK YGTMPLNKVV QPAFKLARDG FIVNDALADD LKTYGSEVLP
    210 220 230 240 250
    NHENSKAIFW KEGEPLKKGD TLVQANLAKS LEMIAENGPD EFYKGTIAEQ
    260 270 280 290 300
    IAQEMQKNGG LITKEDLAAY KAVERTPISG DYRGYQVYSM PPPSSGGIHI
    310 320 330 340 350
    VQILNILENF DMKKYGFGSA DAMQIMAEAE KYAYADRSEY LGDPDFVKVP
    360 370 380 390 400
    WQALTNKAYA KSIADQIDIN KAKPSSEIRP GKLAPYESNQ TTHYSVVDKD
    410 420 430 440 450
    GNAVAVTYTL NTTFGTGIVA GESGILLNNQ MDDFSAKPGV PNVYGLVGGD
    460 470 480 490 500
    ANAVGPNKRP LSSMSPTIVV KDGKTWLVTG SPGGSRIITT VLQMVVNSID
    510 520 530 540 550
    YGLNVAEATN APRFHHQWLP DELRVEKGFS PDTLKLLEAK GQKVALKEAM
    560 570 580
    GSTQSIMVGP DGELYGASDP RSVDDLTAGY
    Length:580
    Mass (Da):61,768
    Last modified:November 1, 1990 - 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:i772F652EBA2A5F00
    GO

    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
    M28722 Genomic DNA Translation: AAA23869.1
    U18997 Genomic DNA Translation: AAA58245.1
    U00096 Genomic DNA Translation: AAC76472.1
    AP009048 Genomic DNA Translation: BAE77846.1
    U00039 Genomic DNA Translation: AAB18422.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    JV0028 EKECEX

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417904.1, NC_000913.3
    WP_000595082.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC76472; AAC76472; b3447
    BAE77846; BAE77846; BAE77846

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947947

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW3412
    eco:b3447

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|511145.12.peg.3544

    <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
    M28722 Genomic DNA Translation: AAA23869.1
    U18997 Genomic DNA Translation: AAA58245.1
    U00096 Genomic DNA Translation: AAC76472.1
    AP009048 Genomic DNA Translation: BAE77846.1
    U00039 Genomic DNA Translation: AAB18422.1
    PIRiJV0028 EKECEX
    RefSeqiNP_417904.1, NC_000913.3
    WP_000595082.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2DBUX-ray1.95A/C25-390[»]
    B/D391-580[»]
    2DBWX-ray1.80A/C25-390[»]
    B/D391-580[»]
    2DBXX-ray1.70A/C25-390[»]
    B/D391-580[»]
    2DG5X-ray1.60A/C25-390[»]
    B/D391-580[»]
    2E0WX-ray2.55A/B25-580[»]
    2E0XX-ray1.95A/C25-390[»]
    B/D391-580[»]
    2E0YX-ray2.02A/C25-390[»]
    B/D391-580[»]
    2Z8IX-ray1.65A/C25-390[»]
    B/D391-580[»]
    2Z8JX-ray2.05A/C25-390[»]
    B/D391-580[»]
    2Z8KX-ray1.65A/C25-390[»]
    B/D391-580[»]
    5B5TX-ray1.70A/C25-390[»]
    B/D391-580[»]
    ProteinModelPortaliP18956
    SMRiP18956
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261666, 434 interactors
    DIPiDIP-9758N
    IntActiP18956, 1 interactor
    STRINGi316385.ECDH10B_3621

    Protein family/group databases

    MEROPSiT03.001

    Proteomic databases

    PaxDbiP18956
    PRIDEiP18956

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76472; AAC76472; b3447
    BAE77846; BAE77846; BAE77846
    GeneIDi947947
    KEGGiecj:JW3412
    eco:b3447
    PATRICifig|511145.12.peg.3544

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0369
    EcoGeneiEG10374 ggt

    Phylogenomic databases

    eggNOGiENOG4105CFB Bacteria
    COG0405 LUCA
    HOGENOMiHOG000175617
    InParanoidiP18956
    KOiK00681
    PhylomeDBiP18956

    Enzyme and pathway databases

    UniPathwayi
    UPA00204

    BioCyciEcoCyc:EG10374-MONOMER
    MetaCyc:EG10374-MONOMER
    BRENDAi2.3.2.2 2026
    3.4.19.13 2026
    SABIO-RKiP18956

    Miscellaneous databases

    EvolutionaryTraceiP18956

    Protein Ontology

    More...
    PROi
    PR:P18956

    Family and domain databases

    InterProiView protein in InterPro
    IPR000101 GGT_peptidase
    IPR029055 Ntn_hydrolases_N
    SUPFAMiSSF56235 SSF56235, 1 hit
    TIGRFAMsiTIGR00066 g_glut_trans, 1 hit
    PROSITEiView protein in PROSITE
    PS00462 G_GLU_TRANSPEPTIDASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiGGT_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: P18956
    Secondary accession number(s): Q2M7B0
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: December 5, 2018
    This is version 162 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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