PAT_SALTI
ID PAT_SALTI Reviewed; 459 AA.
AC Q8Z3L9; Q7C743;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Putrescine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01276};
DE Short=PAT {ECO:0000255|HAMAP-Rule:MF_01276};
DE Short=PATase {ECO:0000255|HAMAP-Rule:MF_01276};
DE EC=2.6.1.82 {ECO:0000255|HAMAP-Rule:MF_01276};
DE AltName: Full=Cadaverine transaminase {ECO:0000255|HAMAP-Rule:MF_01276};
DE AltName: Full=Diamine transaminase {ECO:0000255|HAMAP-Rule:MF_01276};
DE EC=2.6.1.29 {ECO:0000255|HAMAP-Rule:MF_01276};
DE AltName: Full=Putrescine transaminase {ECO:0000255|HAMAP-Rule:MF_01276};
DE AltName: Full=Putrescine--2-oxoglutaric acid transaminase {ECO:0000255|HAMAP-Rule:MF_01276};
GN Name=patA {ECO:0000255|HAMAP-Rule:MF_01276};
GN OrderedLocusNames=STY3396, t3138;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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:0000255|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:0000255|HAMAP-Rule:MF_01276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18218;
CC Evidence={ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_01276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12269;
CC Evidence={ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61625;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01276};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01276};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC aminobutanal from putrescine (transaminase route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01276}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. Putrescine aminotransferase subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01276}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO70680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD07742.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL513382; CAD07742.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014613; AAO70680.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_457608.3; NC_003198.1.
DR RefSeq; WP_001536702.1; NZ_WNTL01000004.1.
DR AlphaFoldDB; Q8Z3L9; -.
DR SMR; Q8Z3L9; -.
DR STRING; 220341.16504294; -.
DR EnsemblBacteria; AAO70680; AAO70680; t3138.
DR KEGG; stt:t3138; -.
DR KEGG; sty:STY3396; -.
DR PATRIC; fig|220341.7.peg.3458; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OMA; DVFPRFA; -.
DR UniPathway; UPA00188; UER00290.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
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; 3.40.640.10; -; 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; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
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; Pyridoxal phosphate; Transferase.
FT CHAIN 1..459
FT /note="Putrescine aminotransferase"
FT /id="PRO_0000269735"
FT BINDING 150..151
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:0000255|HAMAP-Rule:MF_01276"
FT BINDING 274
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:0000255|HAMAP-Rule:MF_01276"
FT BINDING 332
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01276"
FT MOD_RES 300
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01276"
SQ SEQUENCE 459 AA; 49709 MW; 5F278B29EADEBD5C CRC64;
MNRLPSSASA LACSAHALNL IEKRTLNHEE MKALNREVID YFKEHVNPGF LEYRKSVTAG
GDYGAVEWQA GSLNTLVDTQ GQEFIDCLGG FGIFNVGHRN PVVVSAVQNQ LAKQPLHSQE
LLDPLRAMLA KTLAALTPGK LKYSFFCNSG TESVEAALKL AKAYQSPRGK FTFIATSGAF
HGKSLGALSA TAKSTFRRPF MPLLPGFRHV PFGNIDAMSM AFSEGKKTGD EIAAVILEPI
QGEGGVILPP QGYLTEVRKL CDEFGALMIL DEVQTGMGRT GKMFACEHEN VQPDILCLAK
ALGGGVMPIG ATIATEEVFS VLFDNPFLHT TTFGGNPLAC AAALATINVL LEQNLPAQAE
QKGDTLLDGF RQLAREYPNL VHEARGKGML MAIEFVDNET GYRFASEMFR QRVLVAGTLN
NAKTIRIEPP LTLTIELCEQ VLKSARNALA AMQVSVEEV
