PAT_ECOLU
ID PAT_ECOLU Reviewed; 459 AA.
AC B7ND61;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 85.
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=ECUMN_3556;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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=CAR14711.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CU928163; CAR14711.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001309772.1; NC_011751.1.
DR AlphaFoldDB; B7ND61; -.
DR SMR; B7ND61; -.
DR STRING; 585056.ECUMN_3556; -.
DR EnsemblBacteria; CAR14711; CAR14711; ECUMN_3556.
DR GeneID; 67414980; -.
DR KEGG; eum:ECUMN_3556; -.
DR PATRIC; fig|585056.7.peg.3732; -.
DR HOGENOM; CLU_016922_10_0_6; -.
DR UniPathway; UPA00188; UER00290.
DR Proteomes; UP000007097; 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_0000379555"
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; 49604 MW; 85CDB4838443B89A CRC64;
MNRLPSSASA LACSAHALNL IEKRTLDHEE MKALNREVIE YFKEHVNPGF LEYRKSVTAG
GDYGAVEWQA GGLNTLVDTQ GQEFIDCLGG FGIFNVGHRN PVVVSAVQNQ LAKQPLHSQE
LLDPLRAMLA KTLAALTPGK LKYSFFCNSG TESVEAALKL AKAYQSPRGK FTFIATSGAF
HGKSLGALSA TAKSTFRKPF MPLLPGFRHV PFGNIEAMRT ALSECKKTGD DVAAVILEPI
QGEGGVILPP PGYLTAVRKL CDEFGALMIL DEVQTGMGRT GKMFACEHEN VQPDILCLAK
ALGGGVMPIG ATIATEEVFS VLFDNPFLHT TTFGGNPLAC AAALATINVL LEQNLPAQAE
QKGDMLLDGF RQLAREYPDL VQEARGKGML MAIEFVDNEI GYNFASEMFR QRVLVAGTLN
NAKTIRIEPP LTLTIEQCEL VIKAARKALA AMRVSVEEA
