AC MF_01276; DC Protein; auto TR HAMAP; MF_01276; -; 1; level=0 XX Names: Putres_aminotrans_3 XX ID PAT DE RecName: Full=Putrescine aminotransferase; DE Short=PAT; DE Short=PATase; DE EC=2.6.1.82; DE AltName: Full=Cadaverine transaminase; DE AltName: Full=Diamine transaminase; DE EC=2.6.1.29; DE AltName: Full=Putrescine transaminase; DE AltName: Full=Putrescine--2-oxoglutaric acid transaminase; GN Name=patA; XX CC -!- FUNCTION: Catalyzes the aminotransferase reaction from putrescine to 2- CC oxoglutarate, leading to glutamate and 4-aminobutanal, which CC spontaneously cyclizes to form 1-pyrroline. This is the first step in CC one of two pathways for putrescine degradation, where putrescine is CC converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4- CC aminobutanal. Also functions as a cadaverine transaminase in a a L- CC lysine degradation pathway to succinate that proceeds via cadaverine, CC glutarate and L-2-hydroxyglutarate. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + an alkane-alpha,omega-diamine = an omega- CC aminoaldehyde + L-glutamate; Xref=Rhea:RHEA:18217, Rhea:RHEA- CC COMP:9766, Rhea:RHEA-COMP:12750, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:70977, ChEBI:CHEBI:133427; CC EC=2.6.1.29; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18218; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + putrescine = 1-pyrroline + H2O + L-glutamate; CC Xref=Rhea:RHEA:12268, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:36781, ChEBI:CHEBI:326268; CC EC=2.6.1.82; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12269; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + cadaverine = 5-aminopentanal + L-glutamate; CC Xref=Rhea:RHEA:61624, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:58384, ChEBI:CHEBI:144896; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61625; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4- CC aminobutanal from putrescine (transaminase route): step 1/1. CC -!- PATHWAY: Amino-acid degradation. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. Putrescine aminotransferase subfamily. XX DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1; trigger=no DR Pfam; PF00202; Aminotran_3; 1; trigger=no DR NCBIfam; TIGR03372; putres_am_tran; 1; trigger=no DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1; trigger=no XX KW Aminotransferase KW Pyridoxal phosphate KW Transferase XX GO GO:0033094; F:putrescine--2-oxoglutarate transaminase activity GO GO:0030170; F:pyridoxal phosphate binding GO GO:0009447; P:putrescine catabolic process GO GO:0019477; P:L-lysine catabolic process XX FT From: PAT_ECOLI (P42588) FT BINDING 150..151 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: G-T FT BINDING 274 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT Condition: Q FT BINDING 332 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT Condition: T FT MOD_RES 300 FT /note="N6-(pyridoxal phosphate)lysine" FT Condition: K XX Size: 459-468; Related: None; Template: P42588; Scope: Bacteria; Enterobacterales Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.23 2023/10/13 //