PAT_SHIFL
ID PAT_SHIFL Reviewed; 459 AA.
AC Q83JJ8; Q7UBI3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 134.
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=SF3114, S3320;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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=AAN44587.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP18399.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005674; AAN44587.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP18399.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_708880.4; NC_004337.2.
DR RefSeq; WP_005051020.1; NZ_WPGW01000031.1.
DR AlphaFoldDB; Q83JJ8; -.
DR SMR; Q83JJ8; -.
DR STRING; 198214.SF3114; -.
DR EnsemblBacteria; AAN44587; AAN44587; SF3114.
DR EnsemblBacteria; AAP18399; AAP18399; S3320.
DR GeneID; 1027200; -.
DR KEGG; sfl:SF3114; -.
DR KEGG; sfx:S3320; -.
DR PATRIC; fig|198214.7.peg.3697; -.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OrthoDB; 572533at2; -.
DR UniPathway; UPA00188; UER00290.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome; Transferase.
FT CHAIN 1..459
FT /note="Putrescine aminotransferase"
FT /id="PRO_0000269738"
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
