Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD

Gene

puuD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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. NADP/NAD-dependent 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)DescriptionActionsGraphical viewLength
    Active sitei114NucleophilePROSITE-ProRule annotation1
    Active sitei222PROSITE-ProRule annotation1
    Active sitei224PROSITE-ProRule annotation1

    GO - Molecular functioni

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

    GO - Biological processi

    • putrescine catabolic process Source: EcoCyc

    Keywordsi

    Molecular functionHydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:G6645-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13909 puuD

    Pathology & Biotechi

    Disruption phenotypei

    Cells lose the hydrolase activity.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi114C → A: Lacks the PuuD activity. The expression level is similar to that of the wild-type. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000971101 – 254Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuDAdd BLAST254

    Proteomic databases

    PaxDbiP76038
    PRIDEiP76038

    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

    BioGridi426014129 interactors.
    IntActiP76038 1 interactor.
    STRINGi316385.ECDH10B_1415

    Structurei

    3D structure databases

    ProteinModelPortaliP76038
    SMRiP76038
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini16 – 250Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd BLAST235

    Sequence similaritiesi

    Belongs to the peptidase C26 family.Curated

    Phylogenomic databases

    eggNOGiENOG4108Z86 Bacteria
    COG2071 LUCA
    HOGENOMiHOG000035715
    InParanoidiP76038
    KOiK09473
    OMAiNVEPHRY
    PhylomeDBiP76038

    Family and domain databases

    Gene3Di3.40.50.8801 hit
    InterProiView protein in InterPro
    IPR029062 Class_I_gatase-like
    IPR017926 GATASE
    IPR011697 Peptidase_C26
    PfamiView protein in Pfam
    PF07722 Peptidase_C26, 1 hit
    SUPFAMiSSF52317 SSF52317, 1 hit
    PROSITEiView protein in PROSITE
    PS51273 GATASE_TYPE_1, 1 hit

    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
    PATRICifig|511145.12.peg.1354

    Similar proteinsi

    Entry informationi

    Entry nameiPUUD_ECOLI
    AccessioniPrimary (citable) accession number: P76038
    Secondary accession number(s): P77761
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: December 15, 1998
    Last modified: March 28, 2018
    This is version 134 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome