A0A6C8GBQ6 · A0A6C8GBQ6_SALIN

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 site159-160pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site283pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site341pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners

GO annotations

AspectTerm
Molecular Functiondiamine transaminase activity
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
      patA
    • ORF names
      SEENIN0B_03431

Organism names

Accessions

  • Primary accession
    A0A6C8GBQ6

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue309N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    468
  • Mass (Da)
    50,681
  • Last updated
    2020-06-17 v1
  • Checksum
    8505DF001B32A5C8
MIHGPLELILNRLPSSASALACSAHALNLIEKRTLNHEEMKALNREVIDYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRRPFMPLLPGFRHVPFGNIDAMSMAFSEGKKTGDEIAAVILEPIQGEGGVILPPQGYLTEVRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPAQAEQKGDTLLDGFRQLAREYPNLVHDARGKGMLMAIEFVDNETGYRFASEMFRQRVLVAGTLNNAKTIRIEPPLTLTIELCEQVLKSARNALAAMQVSVEEV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AFYI01000002
EMBL· GenBank· DDBJ
EHB43515.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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