ID A0A5I0NEP7_SALET Unreviewed; 476 AA. AC A0A5I0NEP7; DT 11-DEC-2019, integrated into UniProtKB/TrEMBL. DT 11-DEC-2019, sequence version 1. DT 28-JUN-2023, 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=ygjG {ECO:0000313|EMBL:HAE0918964.1}; GN Synonyms=patA {ECO:0000256|HAMAP-Rule:MF_01276}; GN ORFNames=EKG43_08255 {ECO:0000313|EMBL:ECA3600882.1}, G2172_19080 GN {ECO:0000313|EMBL:HAE0918964.1}; OS Salmonella enterica subsp. enterica serovar Coeln. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=399584 {ECO:0000313|EMBL:HAE0918964.1}; RN [1] {ECO:0000313|EMBL:HAE0918964.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sam_adb27551-3cab-45c5-aafd-87b47b435c68 RC {ECO:0000313|EMBL:HAE0918964.1}; RX PubMed=30286803; RA Souvorov A., Agarwala R., Lipman D.J.; RT "SKESA: strategic k-mer extension for scrupulous assemblies."; RL Genome Biol. 19:153-150(2018). RN [2] {ECO:0000313|EMBL:ECA3600882.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=636263 {ECO:0000313|EMBL:ECA3600882.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:HAE0918964.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sam_adb27551-3cab-45c5-aafd-87b47b435c68 RC {ECO:0000313|EMBL:HAE0918964.1}; RG NCBI Pathogen Detection Project; RL Submitted (JAN-2019) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HAE0918964.1}. 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; AAHUCI010000004; ECA3600882.1; -; Genomic_DNA. DR EMBL; DAAQUJ010000007; HAE0918964.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5I0NEP7; -. DR UniPathway; UPA00188; UER00290. DR GO; GO:0033094; F:butane-1,4-diamine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019161; F:diamine transaminase activity; IEA:UniProtKB-EC. 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; IPR017747; Putrescine_aminotransferase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. 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 TIGRFAMs; TIGR03372; putres_am_tran; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01276, KW ECO:0000313|EMBL:HAE0918964.1}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_01276}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01276, KW ECO:0000313|EMBL:HAE0918964.1}. FT BINDING 167..168 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 291 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 349 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 317 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01276" SQ SEQUENCE 476 AA; 51727 MW; 52F41028ABA441DA CRC64; MQYLIQYHVI HGPLELILNR LPSSASALAC SAHALNLIEK RTLNHEEMKA LNREVIDYFK EHVNPGFLEY RKSVTAGGDY GAVEWQAGSL NTLVDTQGQE FIDCLGGFGI FNVGHRNPVV VSAVQNQLAK QPLHSQELLD PLRAMLAKTL AALTPGKLKY SFFCNSGTES VEAALKLAKA YQSPRGKFTF IATSGAFHGK SLGALSATAK STFRRPFMPL LPGFRHVPFG NIDAMSMAFS EGKKTGDEIA AVILEPIQGE GGVILPPQGY LTEVRKLCDE FGALMILDEV QTGMGRTGKM FACEHENVQP DILCLAKALG GGVMPIGATI ATEEVFSVLF DNPFLHTTTF GGNPLACAAA LATINVLLEQ NLPAQAEQKG DTLLDGFRQL AREYPNLVHD ARGKGMLMAI EFVDNETGYR FASEMFRQRV LVAGTLNNAK TIRIEPPLTL TIELCEQVLK SARNALAAMQ VSVEEV //