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Protein

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD

Gene

puuD

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

Functioni

Involved in the breakdown of putrescine via hydrolysis of the gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate.2 Publications

Catalytic activityi

4-(gamma-L-glutamylamino)butanoate + H2O = 4-aminobutanoate + L-glutamate.1 Publication

Kineticsi

  1. KM=2.93 mM for gamma-glutamyl-gamma-aminobutyrate2 Publications
  2. KM=18.5 mM for gamma-glutamylputrescine2 Publications

    pH dependencei

    Optimum pH is between 8.5 and 9.2 Publications

    Pathwayi: putrescine degradation

    This protein is involved in step 4 of the subpathway that synthesizes 4-aminobutanoate from putrescine.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Gamma-glutamylputrescine synthetase PuuA (puuA)
    2. Gamma-glutamylputrescine oxidoreductase (puuB)
    3. Aldehyde dehydrogenase PuuC (puuC)
    4. Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (puuD)
    This subpathway is part of the pathway putrescine degradation, which is itself part of Amine and polyamine degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-aminobutanoate from putrescine, the pathway putrescine degradation and in Amine and polyamine degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei114 – 1141NucleophilePROSITE-ProRule annotation
    Active sitei222 – 2221PROSITE-ProRule annotation
    Active sitei224 – 2241PROSITE-ProRule annotation

    GO - Molecular functioni

    • gamma-glutamyl-gamma-aminobutyrate hydrolase activity Source: EcoCyc

    GO - Biological processi

    • glutamine metabolic process Source: InterPro
    • putrescine catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:G6645-MONOMER.
    ECOL316407:JW1291-MONOMER.
    MetaCyc:G6645-MONOMER.
    BRENDAi3.5.1.94. 2165.
    UniPathwayiUPA00188; UER00883.

    Protein family/group databases

    MEROPSiC26.961.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (EC:3.5.1.94)
    Short name:
    Gamma-Glu-GABA hydrolase
    Gene namesi
    Name:puuD
    Synonyms:ycjL
    Ordered Locus Names:b1298, JW1291
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13909. puuD.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Disruption phenotypei

    Cells lose the hydrolase activity.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1141C → A: Lacks the PuuD activity. The expression level is similar to that of the wild-type. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 254254Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuDPRO_0000097110Add
    BLAST

    Proteomic databases

    PaxDbiP76038.

    Expressioni

    Inductioni

    Induced by putrescine and nutrient starvation. Repressed by PuuR and low aeration condition. Repressed at the exponential phase and highly induced in early stationary phase.2 Publications

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi4260141. 29 interactions.
    IntActiP76038. 1 interaction.
    STRINGi511145.b1298.

    Structurei

    3D structure databases

    ProteinModelPortaliP76038.
    SMRiP76038. Positions 26-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 250235Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C26 family.Curated
    Contains 1 glutamine amidotransferase type-1 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG4108Z86. Bacteria.
    COG2071. LUCA.
    HOGENOMiHOG000035715.
    InParanoidiP76038.
    KOiK09473.
    OMAiGFITACR.
    PhylomeDBiP76038.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR011697. Peptidase_C26.
    [Graphical view]
    PfamiPF07722. Peptidase_C26. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P76038-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MENIMNNPVI GVVMCRNRLK GHATQTLQEK YLNAIIHAGG LPIALPHALA
    60 70 80 90 100
    EPSLLEQLLP KLDGIYLPGS PSNVQPHLYG ENGDEPDADP GRDLLSMAII
    110 120 130 140 150
    NAALERRIPI FAICRGLQEL VVATGGSLHR KLCEQPELLE HREDPELPVE
    160 170 180 190 200
    QQYAPSHEVQ VEEGGLLSAL LPECSNFWVN SLHGQGAKVV SPRLRVEARS
    210 220 230 240 250
    PDGLVEAVSV INHPFALGVQ WHPEWNSSEY ALSRILFEGF ITACQHHIAE

    KQRL
    Length:254
    Mass (Da):28,013
    Last modified:December 15, 1998 - v2
    Checksum:iED183250300CCB42
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC74380.2.
    AP009048 Genomic DNA. Translation: BAA14858.1.
    PIRiE64878.
    RefSeqiNP_415814.4. NC_000913.3.
    WP_001300506.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74380; AAC74380; b1298.
    BAA14858; BAA14858; BAA14858.
    GeneIDi945882.
    KEGGiecj:JW1291.
    eco:b1298.
    PATRICi32117868. VBIEscCol129921_1354.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC74380.2.
    AP009048 Genomic DNA. Translation: BAA14858.1.
    PIRiE64878.
    RefSeqiNP_415814.4. NC_000913.3.
    WP_001300506.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP76038.
    SMRiP76038. Positions 26-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260141. 29 interactions.
    IntActiP76038. 1 interaction.
    STRINGi511145.b1298.

    Protein family/group databases

    MEROPSiC26.961.

    Proteomic databases

    PaxDbiP76038.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74380; AAC74380; b1298.
    BAA14858; BAA14858; BAA14858.
    GeneIDi945882.
    KEGGiecj:JW1291.
    eco:b1298.
    PATRICi32117868. VBIEscCol129921_1354.

    Organism-specific databases

    EchoBASEiEB3668.
    EcoGeneiEG13909. puuD.

    Phylogenomic databases

    eggNOGiENOG4108Z86. Bacteria.
    COG2071. LUCA.
    HOGENOMiHOG000035715.
    InParanoidiP76038.
    KOiK09473.
    OMAiGFITACR.
    PhylomeDBiP76038.

    Enzyme and pathway databases

    UniPathwayiUPA00188; UER00883.
    BioCyciEcoCyc:G6645-MONOMER.
    ECOL316407:JW1291-MONOMER.
    MetaCyc:G6645-MONOMER.
    BRENDAi3.5.1.94. 2165.

    Miscellaneous databases

    PROiP76038.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR011697. Peptidase_C26.
    [Graphical view]
    PfamiPF07722. Peptidase_C26. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPUUD_ECOLI
    AccessioniPrimary (citable) accession number: P76038
    Secondary accession number(s): P77761
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: December 15, 1998
    Last modified: September 7, 2016
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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. Peptidase families
      Classification of peptidase families and list of entries
    4. 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.