HAMAP logo

HAMAP rule MF_01276

Send feedback

General rule information [?]

Accession MF_01276
Dates 29-NOV-2006 (Created)
1-JUN-2023 (Last updated, Version 22)
Name Putres_aminotrans_3
Scope
Bacteria; Enterobacterales
Template P42588 (PAT_ECOLI)

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
PAT
Protein name
RecName: Full=Putrescine aminotransferase;
Short=PAT;
Short=PATase;
EC 2.6.1.82;
AltName: Full=Cadaverine transaminase;
AltName: Full=Diamine transaminase;
EC 2.6.1.29;
AltName: Full=Putrescine transaminase;
AltName: Full=Putrescine--2-oxoglutaric acid transaminase;
Gene name
patA

Comments [?]

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 RHEA:18217: 2-oxoglutarate + an alkane-alpha,omega-diamine = an omega-aminoaldehyde + L-glutamate
EC 2.6.1.29
PhysiologicalDirection=left-to-right (RHEA:18218)
RHEA:12268: 2-oxoglutarate + putrescine = 1-pyrroline + H2O + L-glutamate
EC 2.6.1.82
PhysiologicalDirection=left-to-right (RHEA:12269)
RHEA:61624: 2-oxoglutarate + cadaverine = 5-aminopentanal + L-glutamate
PhysiologicalDirection=left-to-right (RHEA:61625)
Cofactor pyridoxal 5'-phosphate
Pathway Amine and polyamine degradation; putrescine degradation; 4-aminobutanal from putrescine (transaminase route): step 1/1.
Amino-acid degradation.
Subunit Homodimer.
Similarity Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. Putrescine aminotransferase subfamily.

Keywords [?]


Gene Ontology [?]

GO:0033094; Molecular function: butane-1,4-diamine:2-oxoglutarate aminotransferase activity.
GO:0030170; Molecular function: pyridoxal phosphate binding.
GO:0009447; Biological process: putrescine catabolic process.
GO:0019477; Biological process: L-lysine catabolic process.

Cross-references [?]

PROSITE PS00600; AA_TRANSFER_CLASS_3; 1;
Pfam PF00202; Aminotran_3; 1;
NCBIfam TIGR03372; putres_am_tran; 1;
PIRSF PIRSF000521; Transaminase_4ab_Lys_Orn; 1;

Features [?]

From: PAT_ECOLI (P42588)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     150     151       /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" /ligand_note="ligand shared between dimeric partners" /note="in other chain     G-T  
BINDING     274     274       /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" /ligand_note="ligand shared between dimeric partners" /note="in other chain     Q  
BINDING     332     332       /ligand="pyridoxal 5'-phosphate" /ligand_id="ChEBI:CHEBI:597326" /ligand_note="ligand shared between dimeric partners     T  
MOD_RES     300     300       N6-(pyridoxal phosphate)lysine     K  

Additional information [?]

Size range 459-468 amino acids
Related rules None
Fusion None