B7LQF8 · PAT_ESCF3
- ProteinPutrescine aminotransferase
- GenepatA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids459 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- 2-oxoglutarate + an alkane-alpha,omega-diamine = an omega-aminoaldehyde + L-glutamateThis reaction proceeds in the forward direction.
CHEBI:16810 + an alkane-α,ω-diamine RHEA-COMP:9766 = an ω-aminoaldehyde RHEA-COMP:12750 + CHEBI:29985 - 2-oxoglutarate + cadaverine = 5-aminopentanal + L-glutamateThis reaction proceeds in the forward direction.
Cofactor
Pathway
Amine and polyamine degradation; putrescine degradation; 4-aminobutanal from putrescine (transaminase route): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 150-151 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: GT | ||||||
Binding site | 274 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: Q | ||||||
Binding site | 332 | pyridoxal 5'-phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | diamine transaminase activity | |
Molecular Function | putrescine--2-oxoglutarate transaminase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | L-lysine catabolic process | |
Biological Process | putrescine catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePutrescine aminotransferase
- EC number
- Short namesPAT ; PATase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionB7LQF8
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000379559 | 1-459 | Putrescine aminotransferase | |||
Sequence: MNRLPSSASALACSAHALNLIEKQTLDHEEMKALNREVIEYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGGLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRKPFMPLLPGFRHVPFGHIEAMRTALSECKKTGDDVAAVILEPIQGEGGVILPPPGYLTAVRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPAQAEQKGDMLLDGFRQLAREYPDLVQEARGKGMLMAIEFVDNEIGYNFASEMFRQRVLVAGTLNNAKTIRIEPPLTLTIEQCELVIKAARKALAAMRVSVEEA | ||||||
Modified residue | 300 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Structure
Sequence
- Sequence statusComplete
- Length459
- Mass (Da)49,599
- Last updated2009-07-28 v2
- Checksum9941DA531C2F6B33
Sequence caution
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU928158 EMBL· GenBank· DDBJ | CAQ90518.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |