ID A0A655BXU5_SALET Unreviewed; 468 AA. AC A0A655BXU5; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 29-MAY-2024, entry version 16. DE RecName: Full=Putrescine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01276}; DE Short=PAT {ECO:0000256|HAMAP-Rule:MF_01276}; DE Short=PATase {ECO:0000256|HAMAP-Rule:MF_01276}; DE EC=2.6.1.82 {ECO:0000256|HAMAP-Rule:MF_01276}; DE AltName: Full=Cadaverine transaminase {ECO:0000256|HAMAP-Rule:MF_01276}; DE AltName: Full=Diamine transaminase {ECO:0000256|HAMAP-Rule:MF_01276}; DE EC=2.6.1.29 {ECO:0000256|HAMAP-Rule:MF_01276}; DE AltName: Full=Putrescine transaminase {ECO:0000256|HAMAP-Rule:MF_01276}; DE AltName: Full=Putrescine--2-oxoglutaric acid transaminase {ECO:0000256|HAMAP-Rule:MF_01276}; GN Name=oat {ECO:0000313|EMBL:CNT85510.1}; GN Synonyms=patA {ECO:0000256|HAMAP-Rule:MF_01276}; GN ORFNames=ERS008198_02181 {ECO:0000313|EMBL:CNU20511.1}, GN ERS008207_01160 {ECO:0000313|EMBL:CNT85510.1}; OS Salmonella enterica subsp. enterica serovar Bovismorbificans. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=58097 {ECO:0000313|EMBL:CNT85510.1, ECO:0000313|Proteomes:UP000042394}; RN [1] {ECO:0000313|Proteomes:UP000041314, ECO:0000313|Proteomes:UP000042394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A1104 {ECO:0000313|EMBL:CNU20511.1, RC ECO:0000313|Proteomes:UP000041314}, and D4891 RC {ECO:0000313|EMBL:CNT85510.1, ECO:0000313|Proteomes:UP000042394}; RG Pathogen Informatics; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|HAMAP-Rule:MF_01276}. 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; Evidence={ECO:0000256|HAMAP-Rule:MF_01276}; 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01276}; 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; Evidence={ECO:0000256|HAMAP-Rule:MF_01276}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|HAMAP-Rule:MF_01276}; CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4- CC aminobutanal from putrescine (transaminase route): step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01276}. CC -!- PATHWAY: Amino-acid degradation. {ECO:0000256|HAMAP-Rule:MF_01276}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01276}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. Putrescine aminotransferase subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01276}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CQPD01000009; CNT85510.1; -; Genomic_DNA. DR EMBL; CQPA01000014; CNU20511.1; -; Genomic_DNA. DR AlphaFoldDB; A0A655BXU5; -. DR UniPathway; UPA00188; UER00290. DR Proteomes; UP000041314; Unassembled WGS sequence. DR Proteomes; UP000042394; Unassembled WGS sequence. DR GO; GO:0019161; F:diamine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter. DR GO; GO:0033094; F:putrescine--2-oxoglutarate transaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0019477; P:L-lysine catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd00610; OAT_like; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR HAMAP; MF_01276; Putres_aminotrans_3; 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR017747; Putrescine_aminotransferase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR03372; putres_am_tran; 1. DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1. DR PANTHER; PTHR11986:SF112; PUTRESCINE AMINOTRANSFERASE; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP- KW Rule:MF_01276}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_01276}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01276, ECO:0000313|EMBL:CNT85510.1}. FT BINDING 159..160 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 /evidence="ECO:0000256|HAMAP-Rule:MF_01276" FT BINDING 283 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 /evidence="ECO:0000256|HAMAP-Rule:MF_01276" FT BINDING 341 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01276" FT MOD_RES 309 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01276" SQ SEQUENCE 468 AA; 50681 MW; 8505DF001B32A5C8 CRC64; MIHGPLELIL NRLPSSASAL ACSAHALNLI EKRTLNHEEM KALNREVIDY FKEHVNPGFL EYRKSVTAGG DYGAVEWQAG SLNTLVDTQG QEFIDCLGGF GIFNVGHRNP VVVSAVQNQL AKQPLHSQEL LDPLRAMLAK TLAALTPGKL KYSFFCNSGT ESVEAALKLA KAYQSPRGKF TFIATSGAFH GKSLGALSAT AKSTFRRPFM PLLPGFRHVP FGNIDAMSMA FSEGKKTGDE IAAVILEPIQ GEGGVILPPQ GYLTEVRKLC DEFGALMILD EVQTGMGRTG KMFACEHENV QPDILCLAKA LGGGVMPIGA TIATEEVFSV LFDNPFLHTT TFGGNPLACA AALATINVLL EQNLPAQAEQ KGDTLLDGFR QLAREYPNLV HDARGKGMLM AIEFVDNETG YRFASEMFRQ RVLVAGTLNN AKTIRIEPPL TLTIELCEQV LKSARNALAA MQVSVEEV //