PAT_ECOLI
ID PAT_ECOLI Reviewed; 459 AA.
AC P42588; P78108; Q2M9D3; Q46873;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Putrescine aminotransferase {ECO:0000303|PubMed:12617754};
DE Short=PAT;
DE Short=PATase {ECO:0000303|PubMed:25423189};
DE EC=2.6.1.82 {ECO:0000269|PubMed:12617754, ECO:0000269|PubMed:3510672};
DE AltName: Full=Cadaverine transaminase {ECO:0000305|PubMed:12617754};
DE AltName: Full=Diamine transaminase;
DE EC=2.6.1.29 {ECO:0000269|PubMed:12617754, ECO:0000269|PubMed:30498244, ECO:0000269|PubMed:3510672, ECO:0000305|PubMed:28522202};
DE AltName: Full=Putrescine transaminase {ECO:0000305|PubMed:12617754};
DE AltName: Full=Putrescine--2-oxoglutaric acid transaminase;
DE AltName: Full=Putrescine:2-OG aminotransferase {ECO:0000303|PubMed:12617754};
GN Name=patA {ECO:0000303|PubMed:22636776}; Synonyms=ygjG;
GN OrderedLocusNames=b3073, JW5510;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=3510672; DOI=10.1016/0304-4165(86)90085-1;
RA Prieto-Santos M.I., Martin-Checa J., Balana-Fouce R., Garrido-Pertierra A.;
RT "A pathway for putrescine catabolism in Escherichia coli.";
RL Biochim. Biophys. Acta 880:242-244(1986).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF START CODON,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12617754; DOI=10.1186/1471-2180-3-2;
RA Samsonova N.N., Smirnov S.V., Altman I.B., Ptitsyn L.R.;
RT "Molecular cloning and characterization of Escherichia coli K12 ygjG
RT gene.";
RL BMC Microbiol. 3:2-2(2003).
RN [5]
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=22949197; DOI=10.1107/s1744309112030886;
RA Yeo S.J., Jeong J.H., Yu S.N., Kim Y.G.;
RT "Crystallization and preliminary X-ray crystallographic analysis of YgjG
RT from Escherichia coli.";
RL Acta Crystallogr. F 68:1070-1072(2012).
RN [6]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=22636776; DOI=10.1128/jb.05063-11;
RA Schneider B.L., Reitzer L.;
RT "Pathway and enzyme redundancy in putrescine catabolism in Escherichia
RT coli.";
RL J. Bacteriol. 194:4080-4088(2012).
RN [7]
RP INDUCTION.
RX PubMed=24906570; DOI=10.1007/s00203-014-0991-1;
RA Kim Y.S., Shin H.C., Lee J.H.;
RT "Two mechanisms for putrescine-dependent transcriptional expression of the
RT putrescine aminotransferase gene, ygjG, in Escherichia coli.";
RL Arch. Microbiol. 196:611-618(2014).
RN [8]
RP BIOTECHNOLOGY, AND CATALYTIC ACTIVITY.
RX PubMed=28522202; DOI=10.1016/j.biortech.2017.04.108;
RA Jorge J.M.P., Perez-Garcia F., Wendisch V.F.;
RT "A new metabolic route for the fermentative production of 5-aminovalerate
RT from glucose and alternative carbon sources.";
RL Bioresour. Technol. 245:1701-1709(2017).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=30498244; DOI=10.1038/s41467-018-07563-6;
RA Knorr S., Sinn M., Galetskiy D., Williams R.M., Wang C., Mueller N.,
RA Mayans O., Schleheck D., Hartig J.S.;
RT "Widespread bacterial lysine degradation proceeding via glutarate and L-2-
RT hydroxyglutarate.";
RL Nat. Commun. 9:5071-5071(2018).
RN [10] {ECO:0007744|PDB:4UOX, ECO:0007744|PDB:4UOY}
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) IN COMPLEXES WITH PUTRESCINE AND
RP PLP, COFACTOR, AND PYRIDOXAL-PHOSPHATE AT LYS-300.
RX PubMed=25423189; DOI=10.1371/journal.pone.0113212;
RA Cha H.J., Jeong J.H., Rojviriya C., Kim Y.G.;
RT "Structure of putrescine aminotransferase from Escherichia coli provides
RT insights into the substrate specificity among class III
RT aminotransferases.";
RL PLoS ONE 9:E113212-E113212(2014).
RN [11] {ECO:0007744|PDB:5H7D, ECO:0007744|PDB:5X3F}
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 7-453.
RX PubMed=28572639; DOI=10.1038/s41598-017-02803-z;
RA Youn S.J., Kwon N.Y., Lee J.H., Kim J.H., Choi J., Lee H., Lee J.O.;
RT "Construction of novel repeat proteins with rigid and predictable
RT structures using a shared helix method.";
RL Sci. Rep. 7:2595-2595(2017).
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 (PubMed:12617754,
CC PubMed:3510672). This is the first step in one of two pathways for
CC putrescine degradation, where putrescine is converted into 4-
CC aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal, which
CC allows E.coli to grow on putrescine as the sole nitrogen source
CC (PubMed:3510672, PubMed:22636776). Also functions as a cadaverine
CC transaminase in a a L-lysine degradation pathway to succinate that
CC proceeds via cadaverine, glutarate and L-2-hydroxyglutarate
CC (PubMed:12617754, PubMed:30498244). Is also able to transaminate
CC spermidine, in lower extent, but not ornithine. Alpha-ketobutyrate and
CC pyruvate can also act as amino acceptors, although much less
CC efficiently (PubMed:12617754). {ECO:0000269|PubMed:12617754,
CC ECO:0000269|PubMed:22636776, ECO:0000269|PubMed:30498244,
CC ECO:0000269|PubMed:3510672}.
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:0000269|PubMed:12617754,
CC ECO:0000269|PubMed:30498244, ECO:0000269|PubMed:3510672,
CC ECO:0000305|PubMed:28522202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18218;
CC Evidence={ECO:0000305|PubMed:12617754, ECO:0000305|PubMed:30498244,
CC ECO:0000305|PubMed:3510672};
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:0000269|PubMed:12617754,
CC ECO:0000269|PubMed:3510672};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12269;
CC Evidence={ECO:0000305|PubMed:12617754, ECO:0000305|PubMed:3510672};
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;
CC Evidence={ECO:0000269|PubMed:12617754, ECO:0000269|PubMed:30498244,
CC ECO:0000305|PubMed:28522202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61625;
CC Evidence={ECO:0000305|PubMed:30498244};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:25423189};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.5 uM for putrescine {ECO:0000269|PubMed:3510672};
CC pH dependence:
CC Optimum pH is 7.2 (PubMed:3510672). Optimum pH is 9.0. Active at
CC alkaline pH. {ECO:0000269|PubMed:12617754,
CC ECO:0000269|PubMed:3510672};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Highly active from 20 to
CC 80 degrees Celsius. {ECO:0000269|PubMed:12617754};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC aminobutanal from putrescine (transaminase route): step 1/1.
CC {ECO:0000269|PubMed:22636776, ECO:0000269|PubMed:3510672}.
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000305|PubMed:30498244}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22949197}.
CC -!- INDUCTION: Up-regulated under nitrogen starvation conditions.
CC Expression is sigma-54-dependent (PubMed:12617754). Up-regulated by
CC putrescine; this gene expression regulation is controlled by at least
CC two sigma factors: rpoS under excess nitrogen conditions and rpoN under
CC nitrogen-starvation conditions (PubMed:24906570).
CC {ECO:0000269|PubMed:12617754, ECO:0000269|PubMed:24906570}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a high decrease in
CC putrescine aminotransferase activity, but are still able to grow with
CC putrescine as the sole nitrogen source. However, a mutant lacking both
CC patA and either puuA, puuB or puuC cannot grow with putrescine as the
CC sole nitrogen source. {ECO:0000269|PubMed:22636776}.
CC -!- BIOTECHNOLOGY: Can be used in the industrial production of the value-
CC added compound 5-aminovalerate. {ECO:0000269|PubMed:28522202}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. Putrescine aminotransferase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57874.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA89152.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE77123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA57874.1; ALT_INIT; Genomic_DNA.
DR EMBL; U28379; AAA89152.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76108.3; -; Genomic_DNA.
DR EMBL; AP009048; BAE77123.1; ALT_INIT; Genomic_DNA.
DR PIR; F65095; F65095.
DR RefSeq; NP_417544.5; NC_000913.3.
DR RefSeq; WP_001301395.1; NZ_LN832404.1.
DR PDB; 4UOX; X-ray; 2.08 A; A/B/C/D=1-459.
DR PDB; 4UOY; X-ray; 2.30 A; A/B/C/D=1-459.
DR PDB; 5H7D; X-ray; 2.57 A; A/B/C/D/I/J/M/N=7-453.
DR PDB; 5X3F; X-ray; 3.38 A; A=7-453.
DR PDBsum; 4UOX; -.
DR PDBsum; 4UOY; -.
DR PDBsum; 5H7D; -.
DR PDBsum; 5X3F; -.
DR AlphaFoldDB; P42588; -.
DR SMR; P42588; -.
DR BioGRID; 4262398; 13.
DR DIP; DIP-12233N; -.
DR IntAct; P42588; 1.
DR MINT; P42588; -.
DR STRING; 511145.b3073; -.
DR jPOST; P42588; -.
DR PaxDb; P42588; -.
DR PRIDE; P42588; -.
DR EnsemblBacteria; AAC76108; AAC76108; b3073.
DR EnsemblBacteria; BAE77123; BAE77123; BAE77123.
DR GeneID; 947120; -.
DR KEGG; ecj:JW5510; -.
DR KEGG; eco:b3073; -.
DR PATRIC; fig|511145.12.peg.3167; -.
DR EchoBASE; EB2577; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR InParanoid; P42588; -.
DR OMA; DVFPRFA; -.
DR PhylomeDB; P42588; -.
DR BioCyc; EcoCyc:G7596-MON; -.
DR BioCyc; MetaCyc:G7596-MON; -.
DR BRENDA; 2.6.1.82; 2026.
DR SABIO-RK; P42588; -.
DR UniPathway; UPA00188; UER00290.
DR PRO; PR:P42588; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0033094; F:butane-1,4-diamine:2-oxoglutarate aminotransferase activity; IDA:EcoCyc.
DR GO; GO:0019161; F:diamine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0019477; P:L-lysine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009447; P:putrescine catabolic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..459
FT /note="Putrescine aminotransferase"
FT /id="PRO_0000120507"
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:0000269|PubMed:25423189"
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:0000269|PubMed:25423189"
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:0000269|PubMed:25423189"
FT MOD_RES 300
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:25423189,
FT ECO:0007744|PDB:4UOY"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 28..45
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:4UOX"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:4UOX"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4UOX"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:4UOX"
FT TURN 273..280
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:4UOX"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:4UOX"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4UOY"
FT HELIX 337..352
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 355..376
FT /evidence="ECO:0007829|PDB:4UOX"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 390..397
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 398..410
FT /evidence="ECO:0007829|PDB:4UOX"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:4UOY"
FT STRAND 419..427
FT /evidence="ECO:0007829|PDB:4UOX"
FT HELIX 435..456
FT /evidence="ECO:0007829|PDB:4UOX"
SQ SEQUENCE 459 AA; 49661 MW; 0B4D42A24627335D CRC64;
MNRLPSSASA LACSAHALNL IEKRTLDHEE MKALNREVIE YFKEHVNPGF LEYRKSVTAG
GDYGAVEWQA GSLNTLVDTQ GQEFIDCLGG FGIFNVGHRN PVVVSAVQNQ LAKQPLHSQE
LLDPLRAMLA KTLAALTPGK LKYSFFCNSG TESVEAALKL AKAYQSPRGK FTFIATSGAF
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
