B7LQF8 · PAT_ESCF3

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.

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.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site150-151pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site274pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site332pyridoxal 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
    • Ordered locus names
      EFER_3025

Organism names

Accessions

  • Primary accession
    B7LQF8

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003795591-459Putrescine aminotransferase
Modified residue300N6-(pyridoxal phosphate)lysine

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    459
  • Mass (Da)
    49,599
  • Last updated
    2009-07-28 v2
  • Checksum
    9941DA531C2F6B33
MNRLPSSASALACSAHALNLIEKQTLDHEEMKALNREVIEYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGGLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRKPFMPLLPGFRHVPFGHIEAMRTALSECKKTGDDVAAVILEPIQGEGGVILPPPGYLTAVRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPAQAEQKGDMLLDGFRQLAREYPDLVQEARGKGMLMAIEFVDNEIGYNFASEMFRQRVLVAGTLNNAKTIRIEPPLTLTIEQCELVIKAARKALAAMRVSVEEA

Sequence caution

The sequence CAQ90518.1 differs from that shown. Reason: Erroneous initiation

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU928158
EMBL· GenBank· DDBJ
CAQ90518.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp