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P50457

- PUUE_ECOLI

UniProt

P50457 - PUUE_ECOLI

Protein

4-aminobutyrate aminotransferase PuuE

Gene

puuE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

    Pyridoxal phosphate.

    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

    Pathwayi

    Sites

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

    GO - Molecular functioni

    1. 4-aminobutyrate transaminase activity Source: EcoCyc
    2. pyridoxal phosphate binding Source: EcoCyc

    GO - Biological processi

    1. gamma-aminobutyric acid metabolic process Source: InterPro
    2. putrescine catabolic process Source: EcoCyc

    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: Chromosome, UP000000625: 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

    Gene expression databases

    GenevestigatoriP50457.

    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.
    KOiK00823.
    OMAiMCGFYAE.
    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]
    PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    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

    MSNNEFHQRR LSATPRGVGV MCNFFAQSAE NATLKDVEGN EYIDFAAGIA    50
    VLNTGHRHPD LVAAVEQQLQ QFTHTAYQIV PYESYVTLAE KINALAPVSG 100
    QAKTAFFTTG AEAVENAVKI ARAHTGRPGV IAFSGGFHGR TYMTMALTGK 150
    VAPYKIGFGP FPGSVYHVPY PSDLHGISTQ DSLDAIERLF KSDIEAKQVA 200
    AIIFEPVQGE GGFNVAPKEL VAAIRRLCDE HGIVMIADEV QSGFARTGKL 250
    FAMDHYADKP DLMTMAKSLA GGMPLSGVVG NANIMDAPAP GGLGGTYAGN 300
    PLAVAAAHAV LNIIDKESLC ERANQLGQRL KNTLIDAKES VPAIAAVRGL 350
    GSMIAVEFND PQTGEPSAAI AQKIQQRALA QGLLLLTCGA YGNVIRFLYP 400
    LTIPDAQFDA AMKILQDALS D 421
    Length:421
    Mass (Da):44,729
    Last modified:October 1, 1996 - v1
    Checksum:iA2C17A885FEBE4EB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_489570.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74384; AAC74384; b1302.
    BAA14871; BAA14871; BAA14871.
    GeneIDi12934532.
    945446.
    KEGGiecj:Y75_p1277.
    eco:b1302.
    PATRICi32117876. VBIEscCol129921_1358.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38543 Genomic DNA. Translation: AAC45301.1 .
    U00096 Genomic DNA. Translation: AAC74384.1 .
    AP009048 Genomic DNA. Translation: BAA14871.1 .
    PIRi A64879.
    RefSeqi NP_415818.1. NC_000913.3.
    YP_489570.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P50457.
    SMRi P50457. Positions 2-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9825N.
    IntActi P50457. 3 interactions.
    MINTi MINT-1256713.
    STRINGi 511145.b1302.

    Proteomic databases

    PaxDbi P50457.
    PRIDEi P50457.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74384 ; AAC74384 ; b1302 .
    BAA14871 ; BAA14871 ; BAA14871 .
    GeneIDi 12934532.
    945446.
    KEGGi ecj:Y75_p1277.
    eco:b1302.
    PATRICi 32117876. VBIEscCol129921_1358.

    Organism-specific databases

    EchoBASEi EB2979.
    EcoGenei EG13187. puuE.

    Phylogenomic databases

    eggNOGi COG0160.
    HOGENOMi HOG000020206.
    KOi K00823.
    OMAi MCGFYAE.
    OrthoDBi EOG6QVRHN.
    PhylomeDBi P50457.

    Enzyme and pathway databases

    UniPathwayi UPA00188 ; UER00293 .
    BioCyci EcoCyc:G6646-MONOMER.
    ECOL316407:JW1295-MONOMER.
    MetaCyc:G6646-MONOMER.
    SABIO-RK P50457.

    Miscellaneous databases

    PROi P50457.

    Gene expression databases

    Genevestigatori P50457.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR004632. 4NH2But_aminotransferase_bac.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR11986. PTHR11986. 1 hit.
    Pfami PF00202. Aminotran_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR00700. GABAtrnsam. 1 hit.
    PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 115 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