ID A0A5I0NEP7_SALET Unreviewed; 476 AA. AC A0A5I0NEP7; DT 11-DEC-2019, integrated into UniProtKB/TrEMBL. DT 11-DEC-2019, sequence version 1. DT 26-FEB-2020, entry version 2. 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 EC=2.6.1.- {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:ECF0053155.1}; GN Synonyms=patA {ECO:0000256|HAMAP-Rule:MF_01276}; GN ORFNames=A4I79_06715 {ECO:0000313|EMBL:ECZ9602196.1}, AVD42_16980 GN {ECO:0000313|EMBL:ECY6039635.1}, E0W27_16555 GN {ECO:0000313|EMBL:ECI7551298.1}, E2L64_09400 GN {ECO:0000313|EMBL:ECG6414605.1}, EX995_13725 GN {ECO:0000313|EMBL:ECD3075008.1}, EXA53_08700 GN {ECO:0000313|EMBL:ECF0053155.1}, EZW89_15370 GN {ECO:0000313|EMBL:ECF0303357.1}, FKW88_05430 GN {ECO:0000313|EMBL:ECG7454314.1}, FLK39_04920 GN {ECO:0000313|EMBL:ECF4908250.1}, FLK41_04945 GN {ECO:0000313|EMBL:ECD8372579.1}; OS Salmonella enterica subsp. enterica serovar Coeln. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=399584 {ECO:0000313|EMBL:ECF0053155.1}; RN [1] {ECO:0000313|EMBL:ECF0053155.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=130358 {ECO:0000313|EMBL:ECG6414605.1}, 170372 RC {ECO:0000313|EMBL:ECZ9602196.1}, 312145 RC {ECO:0000313|EMBL:ECI7551298.1}, 364192 RC {ECO:0000313|EMBL:ECF0303357.1}, 385495 RC {ECO:0000313|EMBL:ECD3075008.1}, 390033 RC {ECO:0000313|EMBL:ECF0053155.1}, 53058 RC {ECO:0000313|EMBL:ECY6039635.1}, 762964 RC {ECO:0000313|EMBL:ECG7454314.1}, 765073 RC {ECO:0000313|EMBL:ECF4908250.1}, and 765633 RC {ECO:0000313|EMBL:ECD8372579.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (FEB-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 + 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|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:ECF0053155.1}. 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; AAIEHF010000023; ECD3075008.1; -; Genomic_DNA. DR EMBL; AAIFZV010000003; ECD8372579.1; -; Genomic_DNA. DR EMBL; AAIJRJ010000013; ECF0053155.1; -; Genomic_DNA. DR EMBL; AAIJVW010000015; ECF0303357.1; -; Genomic_DNA. DR EMBL; AAILJO010000003; ECF4908250.1; -; Genomic_DNA. DR EMBL; AAIPBE010000007; ECG6414605.1; -; Genomic_DNA. DR EMBL; AAIPJZ010000003; ECG7454314.1; -; Genomic_DNA. DR EMBL; AAIWDQ010000014; ECI7551298.1; -; Genomic_DNA. DR EMBL; AALDRF010000018; ECY6039635.1; -; Genomic_DNA. DR EMBL; AALILJ010000005; ECZ9602196.1; -; Genomic_DNA. DR UniPathway; UPA00188; UER00290. DR GO; GO:0033094; F:butane-1,4-diamine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR CDD; cd00610; OAT_like; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 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; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2. DR SUPFAM; SSF53383; SSF53383; 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:ECF0053155.1}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01276, KW ECO:0000256|RuleBase:RU003560}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01276, KW ECO:0000313|EMBL:ECF0053155.1}. FT REGION 167..168 FT /note="Pyridoxal phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01276" FT BINDING 291 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01276" FT BINDING 349 FT /note="Pyridoxal phosphate; shared with dimeric partner" 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 //