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Protein

4-aminobutyrate aminotransferase PuuE

Gene

puuE

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

Functioni

Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA). PuuE is important for utilization of putrescine as the sole nitrogen or carbon source.2 Publications

Catalytic activityi

4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.

Cofactori

Enzyme regulationi

Completely inhibited by succinate and low-aeration conditions.1 Publication

Kineticsi

  1. KM=0.0577 mM for SSA (at pH 7.8 and at 30 degrees Celsius)1 Publication
  2. KM=1.57 mM for GABA (at pH 7.8 and at 30 degrees Celsius)1 Publication
  3. KM=5.1 mM for KG (at pH 7.8 and at 30 degrees Celsius)1 Publication
  4. KM=18 mM for L-glutamate (at pH 7.8 and at 30 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 9 for the forward reaction which is the transfer reaction of the amino group from GABA to beta-ketoglutarate, and pH 8 for the reverse reaction.1 Publication

    Pathway:iputrescine degradation

    This protein is involved in step 1 of the subpathway that synthesizes succinate semialdehyde from 4-aminobutanoate.
    Proteins known to be involved in this subpathway in this organism are:
    1. 4-aminobutyrate aminotransferase PuuE (puuE)
    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 succinate semialdehyde from 4-aminobutanoate, the pathway putrescine degradation and in Amine and polyamine degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei296 – 2961Pyridoxal phosphateBy similarity

    GO - Molecular functioni

    • 4-aminobutyrate transaminase activity Source: EcoCyc
    • pyridoxal phosphate binding Source: EcoCyc

    GO - Biological processi

    • gamma-aminobutyric acid metabolic process Source: InterPro
    • putrescine catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:G6646-MONOMER.
    ECOL316407:JW1295-MONOMER.
    MetaCyc:G6646-MONOMER.
    SABIO-RKP50457.
    UniPathwayiUPA00188; UER00293.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-aminobutyrate aminotransferase PuuE (EC:2.6.1.19)
    Alternative name(s):
    GABA aminotransferase
    Short name:
    GABA-AT
    Gamma-amino-N-butyrate transaminase
    Short name:
    GABA transaminase
    Glutamate:succinic semialdehyde transaminase
    Gene namesi
    Name:puuE
    Synonyms:goaG
    Ordered Locus Names:b1302, JW1295
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13187. puuE.

    Pathology & Biotechi

    Disruption phenotypei

    Cells show only 35% of the wild-type activity.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi267 – 2671K → A: No GABA-AT activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4214214-aminobutyrate aminotransferase PuuEPRO_0000120388Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei267 – 2671N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiP50457.
    PRIDEiP50457.

    Expressioni

    Inductioni

    By putrescine.1 Publication

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-9825N.
    IntActiP50457. 3 interactions.
    MINTiMINT-1256713.
    STRINGi511145.b1302.

    Structurei

    3D structure databases

    ProteinModelPortaliP50457.
    SMRiP50457. Positions 2-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni110 – 1112Pyridoxal phosphate bindingBy similarity
    Regioni238 – 2414Pyridoxal phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0160.
    HOGENOMiHOG000020206.
    InParanoidiP50457.
    KOiK00823.
    OMAiNLCAEAN.
    OrthoDBiEOG6QVRHN.
    PhylomeDBiP50457.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004632. 4NH2But_aminotransferase_bac.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11986. PTHR11986. 1 hit.
    PfamiPF00202. Aminotran_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR00700. GABAtrnsam. 1 hit.
    PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P50457-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSNNEFHQRR LSATPRGVGV MCNFFAQSAE NATLKDVEGN EYIDFAAGIA
    60 70 80 90 100
    VLNTGHRHPD LVAAVEQQLQ QFTHTAYQIV PYESYVTLAE KINALAPVSG
    110 120 130 140 150
    QAKTAFFTTG AEAVENAVKI ARAHTGRPGV IAFSGGFHGR TYMTMALTGK
    160 170 180 190 200
    VAPYKIGFGP FPGSVYHVPY PSDLHGISTQ DSLDAIERLF KSDIEAKQVA
    210 220 230 240 250
    AIIFEPVQGE GGFNVAPKEL VAAIRRLCDE HGIVMIADEV QSGFARTGKL
    260 270 280 290 300
    FAMDHYADKP DLMTMAKSLA GGMPLSGVVG NANIMDAPAP GGLGGTYAGN
    310 320 330 340 350
    PLAVAAAHAV LNIIDKESLC ERANQLGQRL KNTLIDAKES VPAIAAVRGL
    360 370 380 390 400
    GSMIAVEFND PQTGEPSAAI AQKIQQRALA QGLLLLTCGA YGNVIRFLYP
    410 420
    LTIPDAQFDA AMKILQDALS D
    Length:421
    Mass (Da):44,729
    Last modified:October 1, 1996 - v1
    Checksum:iA2C17A885FEBE4EB
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U38543 Genomic DNA. Translation: AAC45301.1.
    U00096 Genomic DNA. Translation: AAC74384.1.
    AP009048 Genomic DNA. Translation: BAA14871.1.
    PIRiA64879.
    RefSeqiNP_415818.1. NC_000913.3.
    WP_000069229.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74384; AAC74384; b1302.
    BAA14871; BAA14871; BAA14871.
    GeneIDi945446.
    KEGGieco:b1302.
    PATRICi32117876. VBIEscCol129921_1358.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U38543 Genomic DNA. Translation: AAC45301.1.
    U00096 Genomic DNA. Translation: AAC74384.1.
    AP009048 Genomic DNA. Translation: BAA14871.1.
    PIRiA64879.
    RefSeqiNP_415818.1. NC_000913.3.
    WP_000069229.1. NZ_CP010445.1.

    3D structure databases

    ProteinModelPortaliP50457.
    SMRiP50457. Positions 2-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-9825N.
    IntActiP50457. 3 interactions.
    MINTiMINT-1256713.
    STRINGi511145.b1302.

    Proteomic databases

    PaxDbiP50457.
    PRIDEiP50457.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74384; AAC74384; b1302.
    BAA14871; BAA14871; BAA14871.
    GeneIDi945446.
    KEGGieco:b1302.
    PATRICi32117876. VBIEscCol129921_1358.

    Organism-specific databases

    EchoBASEiEB2979.
    EcoGeneiEG13187. puuE.

    Phylogenomic databases

    eggNOGiCOG0160.
    HOGENOMiHOG000020206.
    InParanoidiP50457.
    KOiK00823.
    OMAiNLCAEAN.
    OrthoDBiEOG6QVRHN.
    PhylomeDBiP50457.

    Enzyme and pathway databases

    UniPathwayiUPA00188; UER00293.
    BioCyciEcoCyc:G6646-MONOMER.
    ECOL316407:JW1295-MONOMER.
    MetaCyc:G6646-MONOMER.
    SABIO-RKP50457.

    Miscellaneous databases

    PROiP50457.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004632. 4NH2But_aminotransferase_bac.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11986. PTHR11986. 1 hit.
    PfamiPF00202. Aminotran_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR00700. GABAtrnsam. 1 hit.
    PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Jovanovic G.
      Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "A novel putrescine utilization pathway involves gamma-glutamylated intermediates of Escherichia coli K-12."
      Kurihara S., Oda S., Kato K., Kim H.G., Koyanagi T., Kumagai H., Suzuki H.
      J. Biol. Chem. 280:4602-4608(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A GABA AMINOTRANSFERASE, NOMENCLATURE.
      Strain: K12.
    6. "A putrescine-inducible pathway comprising PuuE-YneI in which gamma-aminobutyrate is degraded into succinate in Escherichia coli K-12."
      Kurihara S., Kato K., Asada K., Kumagai H., Suzuki H.
      J. Bacteriol. 192:4582-4591(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PUTRESCINE DEGRADATION AND AS A GABA AMINOTRANSFERASE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-267, DISRUPTION PHENOTYPE, ENZYME REGULATION, INDUCTION.

    Entry informationi

    Entry nameiPUUE_ECOLI
    AccessioniPrimary (citable) accession number: P50457
    Secondary accession number(s): P78150
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: July 22, 2015
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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

    External Data

    Dasty 3

    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 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.