PAT_SALA4
ID PAT_SALA4 Reviewed; 459 AA.
AC B5F6B4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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}; OrderedLocusNames=SeAg_B3405;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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}.
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DR EMBL; CP001138; ACH48710.1; -; Genomic_DNA.
DR RefSeq; WP_001520281.1; NC_011149.1.
DR AlphaFoldDB; B5F6B4; -.
DR SMR; B5F6B4; -.
DR EnsemblBacteria; ACH48710; ACH48710; SeAg_B3405.
DR KEGG; sea:SeAg_B3405; -.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OMA; DVFPRFA; -.
DR UniPathway; UPA00188; UER00290.
DR Proteomes; UP000008819; 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_1000140278"
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; 49695 MW; 358CFB29EB9AF85D 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 VHDARGKGML MAIEFVDNET GYRFASEMFR QRVLVAGTLN
NAKTIRIEPP LTLTIELCEQ VLKSARNALA AMQVSVEEV
