UniProtKB - P42588 (PAT_ECOLI)
Putrescine aminotransferase
patA
Functioni
Catalyzes the aminotransferase reaction from putrescine to 2-oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline (PubMed:12617754, PubMed:3510672).
This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal, which allows E.coli to grow on putrescine as the sole nitrogen source (PubMed:3510672, PubMed:22636776).
Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate (PubMed:12617754, PubMed:30498244).
Is also able to transaminate spermidine, in lower extent, but not ornithine. Alpha-ketobutyrate and pyruvate can also act as amino acceptors, although much less efficiently (PubMed:12617754).
4 PublicationsCatalytic activityi
- 2-oxoglutarate + an alkane-α,ω-diamine = an ω-aminoaldehyde + L-glutamate1 Publication3 PublicationsEC:2.6.1.291 Publication3 PublicationsThis reaction proceeds in the forward3 Publications direction.
- EC:2.6.1.822 PublicationsThis reaction proceeds in the forward2 Publications direction.
- This reaction proceeds in the forward1 Publication direction.
Cofactori
Kineticsi
- KM=22.5 µM for putrescine1 Publication
pH dependencei
Temperature dependencei
: putrescine degradation Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes 4-aminobutanal from putrescine (transaminase route).2 Publications This subpathway is part of the pathway putrescine degradation, which is itself part of Amine and polyamine degradation.View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-aminobutanal from putrescine (transaminase route), the pathway putrescine degradation and in Amine and polyamine degradation.
Pathwayi: Amino-acid degradation
This protein is involved in Amino-acid degradation.1 PublicationView all proteins of this organism that are known to be involved in Amino-acid degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 274 | Pyridoxal phosphate1 Publication | 1 | |
Binding sitei | 332 | Pyridoxal phosphate; shared with dimeric partner1 Publication | 1 |
GO - Molecular functioni
- butane-1,4-diamine:2-oxoglutarate aminotransferase activity Source: EcoCyc
- diamine transaminase activity Source: UniProtKB-EC
- identical protein binding Source: GO_Central
- pyridoxal phosphate binding Source: EcoCyc
GO - Biological processi
- L-lysine catabolic process Source: UniProtKB-UniRule
- putrescine catabolic process Source: EcoCyc
Keywordsi
Molecular function | Aminotransferase, Transferase |
Ligand | Pyridoxal phosphate |
Enzyme and pathway databases
BioCyci | EcoCyc:G7596-MONOMER |
BRENDAi | 2.6.1.82, 2026 |
SABIO-RKi | P42588 |
UniPathwayi | UPA00188;UER00290 |
Names & Taxonomyi
Protein namesi | Recommended name: Putrescine aminotransferase1 Publication (EC:2.6.1.822 Publications)Short name: PAT Short name: PATase1 Publication Alternative name(s): Cadaverine transaminase1 Publication Diamine transaminase (EC:2.6.1.291 Publication3 Publications) Putrescine transaminase1 Publication Putrescine--2-oxoglutaric acid transaminase Putrescine:2-OG aminotransferase1 Publication |
Gene namesi | Name:patA1 Publication Synonyms:ygjG Ordered Locus Names:b3073, JW5510 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Biotechnological usei
Disruption phenotypei
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000120507 | 1 – 459 | Putrescine aminotransferaseAdd BLAST | 459 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 300 | N6-(pyridoxal phosphate)lysineCombined sources1 Publication | 1 |
Proteomic databases
jPOSTi | P42588 |
PaxDbi | P42588 |
PRIDEi | P42588 |
Expressioni
Inductioni
Interactioni
Subunit structurei
Homodimer.
1 PublicationGO - Molecular functioni
- identical protein binding Source: GO_Central
Protein-protein interaction databases
BioGRIDi | 4262398, 13 interactors |
DIPi | DIP-12233N |
IntActi | P42588, 1 interactor |
MINTi | P42588 |
STRINGi | 511145.b3073 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P42588 |
SMRi | P42588 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 150 – 151 | Pyridoxal phosphate binding1 Publication | 2 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG4992, Bacteria |
HOGENOMi | CLU_016922_10_0_6 |
InParanoidi | P42588 |
OMAi | DVFPRFA |
PhylomeDBi | P42588 |
Family and domain databases
CDDi | cd00610, OAT_like, 1 hit |
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
HAMAPi | MF_01276, Putres_aminotrans_3, 1 hit |
InterProi | View protein in InterPro IPR005814, Aminotrans_3 IPR017747, Putrescine_aminotransferase IPR015424, PyrdxlP-dep_Trfase IPR015421, PyrdxlP-dep_Trfase_major IPR015422, PyrdxlP-dep_Trfase_small |
Pfami | View protein in Pfam PF00202, Aminotran_3, 1 hit |
PIRSFi | PIRSF000521, Transaminase_4ab_Lys_Orn, 1 hit |
SUPFAMi | SSF53383, SSF53383, 1 hit |
TIGRFAMsi | TIGR03372, putres_am_tran, 1 hit |
PROSITEi | View protein in PROSITE PS00600, AA_TRANSFER_CLASS_3, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MNRLPSSASA LACSAHALNL IEKRTLDHEE MKALNREVIE YFKEHVNPGF
60 70 80 90 100
LEYRKSVTAG GDYGAVEWQA GSLNTLVDTQ GQEFIDCLGG FGIFNVGHRN
110 120 130 140 150
PVVVSAVQNQ LAKQPLHSQE LLDPLRAMLA KTLAALTPGK LKYSFFCNSG
160 170 180 190 200
TESVEAALKL AKAYQSPRGK FTFIATSGAF HGKSLGALSA TAKSTFRKPF
210 220 230 240 250
MPLLPGFRHV PFGNIEAMRT ALNECKKTGD DVAAVILEPI QGEGGVILPP
260 270 280 290 300
PGYLTAVRKL CDEFGALMIL DEVQTGMGRT GKMFACEHEN VQPDILCLAK
310 320 330 340 350
ALGGGVMPIG ATIATEEVFS VLFDNPFLHT TTFGGNPLAC AAALATINVL
360 370 380 390 400
LEQNLPAQAE QKGDMLLDGF RQLAREYPDL VQEARGKGML MAIEFVDNEI
410 420 430 440 450
GYNFASEMFR QRVLVAGTLN NAKTIRIEPP LTLTIEQCEL VIKAARKALA
AMRVSVEEA
Sequence cautioni
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U18997 Genomic DNA Translation: AAA57874.1 Different initiation. U28379 Genomic DNA Translation: AAA89152.1 Different initiation. U00096 Genomic DNA Translation: AAC76108.3 AP009048 Genomic DNA Translation: BAE77123.1 Different initiation. |
PIRi | F65095 |
RefSeqi | NP_417544.5, NC_000913.3 WP_001301395.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC76108; AAC76108; b3073 BAE77123; BAE77123; BAE77123 |
GeneIDi | 947120 |
KEGGi | ecj:JW5510 eco:b3073 |
PATRICi | fig|511145.12.peg.3167 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U18997 Genomic DNA Translation: AAA57874.1 Different initiation. U28379 Genomic DNA Translation: AAA89152.1 Different initiation. U00096 Genomic DNA Translation: AAC76108.3 AP009048 Genomic DNA Translation: BAE77123.1 Different initiation. |
PIRi | F65095 |
RefSeqi | NP_417544.5, NC_000913.3 WP_001301395.1, NZ_LN832404.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4UOX | X-ray | 2.08 | A/B/C/D | 1-459 | [»] | |
4UOY | X-ray | 2.30 | A/B/C/D | 1-459 | [»] | |
5H7D | X-ray | 2.57 | A/B/C/D/I/J/M/N | 7-453 | [»] | |
5X3F | X-ray | 3.38 | A | 7-453 | [»] | |
AlphaFoldDBi | P42588 | |||||
SMRi | P42588 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262398, 13 interactors |
DIPi | DIP-12233N |
IntActi | P42588, 1 interactor |
MINTi | P42588 |
STRINGi | 511145.b3073 |
Proteomic databases
jPOSTi | P42588 |
PaxDbi | P42588 |
PRIDEi | P42588 |
Genome annotation databases
EnsemblBacteriai | AAC76108; AAC76108; b3073 BAE77123; BAE77123; BAE77123 |
GeneIDi | 947120 |
KEGGi | ecj:JW5510 eco:b3073 |
PATRICi | fig|511145.12.peg.3167 |
Organism-specific databases
EchoBASEi | EB2577 |
Phylogenomic databases
eggNOGi | COG4992, Bacteria |
HOGENOMi | CLU_016922_10_0_6 |
InParanoidi | P42588 |
OMAi | DVFPRFA |
PhylomeDBi | P42588 |
Enzyme and pathway databases
UniPathwayi | UPA00188;UER00290 |
BioCyci | EcoCyc:G7596-MONOMER |
BRENDAi | 2.6.1.82, 2026 |
SABIO-RKi | P42588 |
Miscellaneous databases
PROi | PR:P42588 |
Family and domain databases
CDDi | cd00610, OAT_like, 1 hit |
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
HAMAPi | MF_01276, Putres_aminotrans_3, 1 hit |
InterProi | View protein in InterPro IPR005814, Aminotrans_3 IPR017747, Putrescine_aminotransferase IPR015424, PyrdxlP-dep_Trfase IPR015421, PyrdxlP-dep_Trfase_major IPR015422, PyrdxlP-dep_Trfase_small |
Pfami | View protein in Pfam PF00202, Aminotran_3, 1 hit |
PIRSFi | PIRSF000521, Transaminase_4ab_Lys_Orn, 1 hit |
SUPFAMi | SSF53383, SSF53383, 1 hit |
TIGRFAMsi | TIGR03372, putres_am_tran, 1 hit |
PROSITEi | View protein in PROSITE PS00600, AA_TRANSFER_CLASS_3, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PAT_ECOLI | |
Accessioni | P42588Primary (citable) accession number: P42588 Secondary accession number(s): P78108, Q2M9D3, Q46873 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | January 9, 2007 | |
Last modified: | May 25, 2022 | |
This is version 157 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families