PAT_SHIF8
ID PAT_SHIF8 Reviewed; 459 AA.
AC Q0T0J2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=SFV_3114;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF05173.1; -; Genomic_DNA.
DR RefSeq; WP_005051020.1; NC_008258.1.
DR AlphaFoldDB; Q0T0J2; -.
DR SMR; Q0T0J2; -.
DR EnsemblBacteria; ABF05173; ABF05173; SFV_3114.
DR KEGG; sfv:SFV_3114; -.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OMA; DVFPRFA; -.
DR BioCyc; SFLE373384:SFV_RS17215-MON; -.
DR UniPathway; UPA00188; UER00290.
DR Proteomes; UP000000659; 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_1000067398"
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; 49659 MW; 1BC5340E512E3E4A CRC64;
MNRLPSSASA LACSAHALNL IEKRTLDHEE MKALNREVIE YFKEHVNPGF LEYRKSVTAG
GDYGAVEWQA GGLNTLVDTQ GQEFIDCLGG FGIFNVGHRN PVVVSAVQNQ LAKQPLHSQE
LLDPLRAMLA KTLAALTPGK LKYSFFCNSG TESVEAALKL AKAYQSPRGK FTFIATSGVF
HGKSLGALSA TAKSTFRKPF MPLLPGFRHV PFGNIEAMRT ALNECKKTGD DVAAVILEPI
QGEGGVILPP PGYLTAVRKL CDEFGALMIL DEVQTGMGRT GKMFACEHEN VQPDILCLAK
ALGGGVMPIG ATIATEEVFS VLFDNPFLHT TTFGGNPLAC AAALATINVL LEQNLPAQAE
QKGDMLLDGF RQLAREYPDL VQEARGKGML MAIEFVDNEI GYNFASEMFR QRVLVAGTLN
NAKTIRIEPP LTLTIEQCEL VIKAARKALA AMRVSVEEA
