ID   A0A5I0NEP7_SALET        Unreviewed;       476 AA.
AC   A0A5I0NEP7;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
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. 19:153-153(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}.
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DR   EMBL; AAHUCI010000004; ECA3600882.1; -; Genomic_DNA.
DR   EMBL; DAAQUJ010000007; HAE0918964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5I0NEP7; -.
DR   UniPathway; UPA00188; UER00290.
DR   GO; GO:0019161; F:diamine transaminase activity; IEA:UniProtKB-EC.
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; 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,
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
//