ID   A0A5I0NEP7_SALET        Unreviewed;       476 AA.
AC   A0A5I0NEP7;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   17-JUN-2020, entry version 4.
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:ECF0053155.1};
GN   Synonyms=patA {ECO:0000256|HAMAP-Rule:MF_01276};
GN   ORFNames=AVD42_16980 {ECO:0000313|EMBL:ECY6039635.1}, E0W27_16555
GN   {ECO:0000313|EMBL:ECI7551298.1}, EKG43_08255
GN   {ECO:0000313|EMBL:ECA3600882.1}, EXA53_08700
GN   {ECO:0000313|EMBL:ECF0053155.1}, FLK39_04920
GN   {ECO:0000313|EMBL:ECF4908250.1};
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=312145 {ECO:0000313|EMBL:ECI7551298.1}, 390033
RC   {ECO:0000313|EMBL:ECF0053155.1}, 53058
RC   {ECO:0000313|EMBL:ECY6039635.1}, 636263
RC   {ECO:0000313|EMBL:ECA3600882.1}, and 765073
RC   {ECO:0000313|EMBL:ECF4908250.1};
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 + 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|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}.
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DR   EMBL; AAHUCI010000004; ECA3600882.1; -; Genomic_DNA.
DR   EMBL; AAIJRJ010000013; ECF0053155.1; -; Genomic_DNA.
DR   EMBL; AAILJO010000003; ECF4908250.1; -; Genomic_DNA.
DR   EMBL; AAIWDQ010000014; ECI7551298.1; -; Genomic_DNA.
DR   EMBL; AALDRF010000018; ECY6039635.1; -; Genomic_DNA.
DR   UniPathway; UPA00188; UER00290.
DR   GO; GO:0033094; F:butane-1,4-diamine:2-oxoglutarate aminotransferase 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; 3.40.640.10; -; 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
//