A0A5I0NEP7 · A0A5I0NEP7_SALET

Function

function

Catalyzes the aminotransferase reaction from putrescine to 2-oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal. Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Amine and polyamine degradation; putrescine degradation; 4-aminobutanal from putrescine (transaminase route): step 1/1.
Amino-acid degradation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site167-168pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site291pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site349pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners

GO annotations

AspectTerm
Molecular Functiondiamine transaminase activity
Molecular Functionidentical protein binding
Molecular Functionputrescine--2-oxoglutarate transaminase activity
Molecular Functionpyridoxal phosphate binding
Biological ProcessL-lysine catabolic process
Biological Processputrescine catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Putrescine aminotransferase
  • EC number
  • Short names
    PAT
    ; PATase
  • Alternative names
    • Cadaverine transaminase
    • Diamine transaminase
      (EC:2.6.1.29
      ) . EC:2.6.1.29 (UniProtKB | ENZYME | Rhea)
    • Putrescine transaminase
    • Putrescine--2-oxoglutaric acid transaminase

Gene names

    • Name
      ygjG
    • Synonyms
      patA
    • ORF names
      EKG43_08255
      , G2172_19080

Organism names

Accessions

  • Primary accession
    A0A5I0NEP7

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue317N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    476
  • Mass (Da)
    51,727
  • Last updated
    2019-12-11 v1
  • Checksum
    52F41028ABA441DA
MQYLIQYHVIHGPLELILNRLPSSASALACSAHALNLIEKRTLNHEEMKALNREVIDYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRRPFMPLLPGFRHVPFGNIDAMSMAFSEGKKTGDEIAAVILEPIQGEGGVILPPQGYLTEVRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPAQAEQKGDTLLDGFRQLAREYPNLVHDARGKGMLMAIEFVDNETGYRFASEMFRQRVLVAGTLNNAKTIRIEPPLTLTIELCEQVLKSARNALAAMQVSVEEV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAHUCI010000004
EMBL· GenBank· DDBJ
ECA3600882.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAQUJ010000007
EMBL· GenBank· DDBJ
HAE0918964.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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