UniProtKB - P19624 (PDXA_ECOLI)
Protein
4-hydroxythreonine-4-phosphate dehydrogenase
Gene
pdxA
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).UniRule annotation2 Publications
Miscellaneous
The active site is located at the dimer interface.UniRule annotation1 Publication
According to PubMed:15026039, PdxA may catalyze both oxidation and decarboxylation reactions that directly lead to AHAP.
Catalytic activityi
- 4-(phosphooxy)-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADHUniRule annotation1 PublicationEC:1.1.1.262UniRule annotation1 Publication
Cofactori
Zn2+UniRule annotation2 Publications, Mg2+UniRule annotation2 Publications, Co2+UniRule annotation2 PublicationsNote: Binds 1 divalent metal cation per subunit. Can use ions such as Zn2+, Mg2+ or Co2+.UniRule annotation2 Publications
Kineticsi
- KM=85 µM for 4-(phosphooxy)-L-threonine (at 0.1 M Tris-HCl and pH 7.5)1 Publication
- KM=113 µM for 4-(phosphooxy)-L-threonine (at 0.1 M phosphate buffer and pH 7.5)1 Publication
- Vmax=2.8 µmol/min/mg enzyme with 4-(phosphooxy)-L-threonine as substrate (at 0.1 M Tris-HCl and pH 7.5)1 Publication
- Vmax=0.66 µmol/min/mg enzyme with 4-(phosphooxy)-L-threonine as substrate (at 0.1 M phosphate buffer and pH 7.5)1 Publication
: pyridoxine 5'-phosphate biosynthesis Pathwayi
This protein is involved in step 4 of the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate.UniRule annotationProteins known to be involved in the 5 steps of the subpathway in this organism are:
- D-erythrose-4-phosphate dehydrogenase (epd), D-erythrose-4-phosphate dehydrogenase (epd)
- Erythronate-4-phosphate dehydrogenase (pdxB), Erythronate-4-phosphate dehydrogenase (pdxB)
- Phosphoserine aminotransferase (serC), Phosphoserine aminotransferase (serC)
- 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA), 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA)
- Pyridoxine 5'-phosphate synthase (pdxJ), Pyridoxine 5'-phosphate synthase (pdxJ)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate, the pathway pyridoxine 5'-phosphate biosynthesis and in Cofactor biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 136 | SubstrateUniRule annotation1 Publication | 1 | |
Binding sitei | 137 | SubstrateUniRule annotation1 Publication | 1 | |
Metal bindingi | 166 | Divalent metal cation; shared with dimeric partnerUniRule annotation1 Publication | 1 | |
Metal bindingi | 211 | Divalent metal cation; shared with dimeric partnerUniRule annotation1 Publication | 1 | |
Metal bindingi | 266 | Divalent metal cation; shared with dimeric partnerUniRule annotation1 Publication | 1 | |
Binding sitei | 274 | SubstrateUniRule annotation1 Publication | 1 | |
Binding sitei | 283 | SubstrateUniRule annotation1 Publication | 1 | |
Binding sitei | 292 | SubstrateUniRule annotation1 Publication | 1 |
GO - Molecular functioni
- 4-hydroxythreonine-4-phosphate dehydrogenase activity Source: EcoCyc
- cobalt ion binding Source: UniProtKB-UniRule
- identical protein binding Source: IntAct
- magnesium ion binding Source: UniProtKB-UniRule
- NAD binding Source: InterPro
- zinc ion binding Source: EcoCyc
GO - Biological processi
- pyridoxal phosphate biosynthetic process Source: EcoCyc
- pyridoxine biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Pyridoxine biosynthesis |
Ligand | Cobalt, Magnesium, Metal-binding, NAD, NADP, Zinc |
Enzyme and pathway databases
BioCyci | EcoCyc:PDXA-MONOMER MetaCyc:PDXA-MONOMER |
BRENDAi | 1.1.1.262, 2026 |
UniPathwayi | UPA00244;UER00312 |
Names & Taxonomyi
Protein namesi | Recommended name: 4-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotation (EC:1.1.1.262UniRule annotation1 Publication)Alternative name(s): 4-(phosphohydroxy)-L-threonine dehydrogenaseUniRule annotation |
Gene namesi | Name:pdxA Ordered Locus Names:b0052, JW0051 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000188804 | 1 – 329 | 4-hydroxythreonine-4-phosphate dehydrogenaseAdd BLAST | 329 |
Proteomic databases
jPOSTi | P19624 |
PaxDbi | P19624 |
PRIDEi | P19624 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotation1 PublicationBinary interactionsi
P19624
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-1112869,EBI-1112869 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4261013, 7 interactors 849317, 5 interactors |
DIPi | DIP-10448N |
IntActi | P19624, 5 interactors |
STRINGi | 511145.b0052 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P19624 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P19624 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1995, Bacteria |
HOGENOMi | CLU_040168_1_0_6 |
InParanoidi | P19624 |
PhylomeDBi | P19624 |
Family and domain databases
HAMAPi | MF_00536, PdxA, 1 hit |
InterProi | View protein in InterPro IPR037510, PdxA IPR005255, PdxA_fam |
PANTHERi | PTHR30004, PTHR30004, 1 hit |
Pfami | View protein in Pfam PF04166, PdxA, 1 hit |
TIGRFAMsi | TIGR00557, pdxA, 1 hit |
i Sequence
Sequence statusi: Complete.
P19624-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA TLLTNRAAML
60 70 80 90 100
GLPLTLRPYS PNSPAQPQTA GTLTLLPVAL RAPVTAGQLA VENGHYVVET
110 120 130 140 150
LARACDGCLN GEFAALITGP VHKGVINDAG IPFTGHTEFF EERSQAKKVV
160 170 180 190 200
MMLATEELRV ALATTHLPLR DIADAITPAL LHEVIAILHH DLRTKFGIAE
210 220 230 240 250
PRILVCGLNP HAGEGGHMGT EEIDTIIPVL NELRAQGMKL NGPLPADTLF
260 270 280 290 300
QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA
310 320
LELAGRGKAD VGSFITALNL AIKMIVNTQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M68521 Genomic DNA Translation: AAA24305.1 U00096 Genomic DNA Translation: AAC73163.1 AP009048 Genomic DNA Translation: BAB96619.1 |
PIRi | JV0026, BVECXA |
RefSeqi | NP_414594.1, NC_000913.3 WP_000241277.1, NZ_STEB01000010.1 |
Genome annotation databases
EnsemblBacteriai | AAC73163; AAC73163; b0052 BAB96619; BAB96619; BAB96619 |
GeneIDi | 944919 |
KEGGi | ecj:JW0051 eco:b0052 |
PATRICi | fig|1411691.4.peg.2231 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M68521 Genomic DNA Translation: AAA24305.1 U00096 Genomic DNA Translation: AAC73163.1 AP009048 Genomic DNA Translation: BAB96619.1 |
PIRi | JV0026, BVECXA |
RefSeqi | NP_414594.1, NC_000913.3 WP_000241277.1, NZ_STEB01000010.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1PS6 | X-ray | 2.25 | A/B | 2-329 | [»] | |
1PS7 | X-ray | 2.47 | A/B/C/D | 1-329 | [»] | |
1PTM | X-ray | 1.96 | A/B | 1-329 | [»] | |
SMRi | P19624 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261013, 7 interactors 849317, 5 interactors |
DIPi | DIP-10448N |
IntActi | P19624, 5 interactors |
STRINGi | 511145.b0052 |
Chemistry databases
DrugBanki | DB02609, 4-Hydroxy-L-Threonine-5-Monophosphate |
Proteomic databases
jPOSTi | P19624 |
PaxDbi | P19624 |
PRIDEi | P19624 |
Genome annotation databases
EnsemblBacteriai | AAC73163; AAC73163; b0052 BAB96619; BAB96619; BAB96619 |
GeneIDi | 944919 |
KEGGi | ecj:JW0051 eco:b0052 |
PATRICi | fig|1411691.4.peg.2231 |
Organism-specific databases
EchoBASEi | EB0685 |
Phylogenomic databases
eggNOGi | COG1995, Bacteria |
HOGENOMi | CLU_040168_1_0_6 |
InParanoidi | P19624 |
PhylomeDBi | P19624 |
Enzyme and pathway databases
UniPathwayi | UPA00244;UER00312 |
BioCyci | EcoCyc:PDXA-MONOMER MetaCyc:PDXA-MONOMER |
BRENDAi | 1.1.1.262, 2026 |
Miscellaneous databases
EvolutionaryTracei | P19624 |
PROi | PR:P19624 |
Family and domain databases
HAMAPi | MF_00536, PdxA, 1 hit |
InterProi | View protein in InterPro IPR037510, PdxA IPR005255, PdxA_fam |
PANTHERi | PTHR30004, PTHR30004, 1 hit |
Pfami | View protein in Pfam PF04166, PdxA, 1 hit |
TIGRFAMsi | TIGR00557, pdxA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PDXA_ECOLI | |
Accessioni | P19624Primary (citable) accession number: P19624 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1991 |
Last sequence update: | February 1, 1991 | |
Last modified: | April 7, 2021 | |
This is version 178 of the entry and version 1 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