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UniProtKB - P05459 (PDXB_ECOLI)
Protein
Erythronate-4-phosphate dehydrogenase
Gene
pdxB
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
UniRule annotationCatalytic activityi
- 4-phospho-D-erythronate + NAD+ = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H+ + NADHUniRule annotationEC:1.1.1.290UniRule annotation
: pyridoxine 5'-phosphate biosynthesis Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate.UniRule annotation1 Publication This subpathway is part of the pathway pyridoxine 5'-phosphate biosynthesis, which is itself part of Cofactor biosynthesis.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 | 45 | SubstrateUniRule annotation | 1 | |
Binding sitei | 66 | SubstrateUniRule annotation | 1 | |
Binding sitei | 146 | NADUniRule annotation | 1 | |
Binding sitei | 175 | NAD; via carbonyl oxygenUniRule annotation | 1 | |
Active sitei | 208 | UniRule annotation | 1 | |
Binding sitei | 232 | NADUniRule annotation | 1 | |
Active sitei | 237 | UniRule annotation | 1 | |
Active sitei | 254 | Proton donorUniRule annotation | 1 | |
Binding sitei | 257 | NAD; via amide nitrogenUniRule annotation | 1 | |
Binding sitei | 258 | SubstrateUniRule annotation | 1 |
GO - Molecular functioni
- 4-phosphoerythronate dehydrogenase activity Source: EcoCyc
- NAD binding Source: EcoCyc
- protein dimerization activity Source: InterPro
GO - Biological processi
- 'de novo' pyridoxal 5'-phosphate biosynthetic process Source: EcoCyc
- pyridoxine biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Pyridoxine biosynthesis |
Ligand | NAD |
Enzyme and pathway databases
BioCyci | EcoCyc:ERYTHRON4PDEHYDROG-MONOMER |
BRENDAi | 1.1.1.290, 2026 |
UniPathwayi | UPA00244;UER00310 |
Names & Taxonomyi
Protein namesi | Recommended name: Erythronate-4-phosphate dehydrogenaseUniRule annotation (EC:1.1.1.290UniRule annotation) |
Gene namesi | Name:pdxBUniRule annotation Ordered Locus Names:b2320, JW2317 |
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
Cytosol
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000075975 | 1 – 378 | Erythronate-4-phosphate dehydrogenaseAdd BLAST | 378 |
Proteomic databases
jPOSTi | P05459 |
PaxDbi | P05459 |
PRIDEi | P05459 |
Expressioni
Inductioni
During growth rate.1 Publication
Interactioni
Subunit structurei
Homodimer.
UniRule annotationGO - Molecular functioni
- protein dimerization activity Source: InterPro
Protein-protein interaction databases
BioGRIDi | 4259616, 24 interactors |
DIPi | DIP-10449N |
IntActi | P05459, 9 interactors |
STRINGi | 511145.b2320 |
Family & Domainsi
Sequence similaritiesi
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily.UniRule annotation
Phylogenomic databases
eggNOGi | COG0111, Bacteria |
HOGENOMi | CLU_019796_4_0_6 |
InParanoidi | P05459 |
PhylomeDBi | P05459 |
Family and domain databases
CDDi | cd12158, ErythrP_dh, 1 hit |
Gene3Di | 3.30.1370.170, 1 hit |
HAMAPi | MF_01825, PdxB, 1 hit |
InterProi | View protein in InterPro IPR006139, D-isomer_2_OHA_DH_cat_dom IPR029753, D-isomer_DH_CS IPR029752, D-isomer_DH_CS1 IPR006140, D-isomer_DH_NAD-bd IPR020921, Erythronate-4-P_DHase IPR024531, Erythronate-4-P_DHase_dimer IPR036291, NAD(P)-bd_dom_sf IPR038251, PdxB_dimer_sf |
Pfami | View protein in Pfam PF00389, 2-Hacid_dh, 1 hit PF02826, 2-Hacid_dh_C, 1 hit PF11890, DUF3410, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00065, D_2_HYDROXYACID_DH_1, 1 hit PS00671, D_2_HYDROXYACID_DH_3, 1 hit |
i Sequence
Sequence statusi: Complete.
P05459-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKILVDENMP YARDLFSRLG EVTAVPGRPI PVAQLADADA LMVRSVTKVN
60 70 80 90 100
ESLLAGKPIK FVGTATAGTD HVDEAWLKQA GIGFSAAPGC NAIAVVEYVF
110 120 130 140 150
SSLLMLAERD GFSLYDRTVG IVGVGNVGRR LQARLEALGI KTLLCDPPRA
160 170 180 190 200
DRGDEGDFRS LDELVQRADI LTFHTPLFKD GPYKTLHLAD EKLIRSLKPG
210 220 230 240 250
AILINACRGA VVDNTALLTC LNEGQKLSVV LDVWEGEPEL NVELLKKVDI
260 270 280 290 300
GTSHIAGYTL EGKARGTTQV FEAYSKFIGH EQHVALDTLL PAPEFGRITL
310 320 330 340 350
HGPLDQPTLK RLVHLVYDVR RDDAPLRKVA GIPGEFDKLR KNYLERREWS
360 370
SLYVICDDAS AASLLCKLGF NAVHHPAR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M29962 Genomic DNA Translation: AAA24308.1 U76961 Genomic DNA Translation: AAB36530.1 U00096 Genomic DNA Translation: AAC75380.1 AP009048 Genomic DNA Translation: BAA16177.1 X02743 Genomic DNA Translation: CAA26520.1 M15541 Genomic DNA Translation: AAA24310.1 |
PIRi | JV0051, DEECPP |
RefSeqi | NP_416823.1, NC_000913.3 WP_000699148.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC75380; AAC75380; b2320 BAA16177; BAA16177; BAA16177 |
GeneIDi | 946785 |
KEGGi | ecj:JW2317 eco:b2320 |
PATRICi | fig|1411691.4.peg.4413 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M29962 Genomic DNA Translation: AAA24308.1 U76961 Genomic DNA Translation: AAB36530.1 U00096 Genomic DNA Translation: AAC75380.1 AP009048 Genomic DNA Translation: BAA16177.1 X02743 Genomic DNA Translation: CAA26520.1 M15541 Genomic DNA Translation: AAA24310.1 |
PIRi | JV0051, DEECPP |
RefSeqi | NP_416823.1, NC_000913.3 WP_000699148.1, NZ_LN832404.1 |
3D structure databases
SMRi | P05459 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4259616, 24 interactors |
DIPi | DIP-10449N |
IntActi | P05459, 9 interactors |
STRINGi | 511145.b2320 |
Proteomic databases
jPOSTi | P05459 |
PaxDbi | P05459 |
PRIDEi | P05459 |
Genome annotation databases
EnsemblBacteriai | AAC75380; AAC75380; b2320 BAA16177; BAA16177; BAA16177 |
GeneIDi | 946785 |
KEGGi | ecj:JW2317 eco:b2320 |
PATRICi | fig|1411691.4.peg.4413 |
Organism-specific databases
EchoBASEi | EB0686 |
Phylogenomic databases
eggNOGi | COG0111, Bacteria |
HOGENOMi | CLU_019796_4_0_6 |
InParanoidi | P05459 |
PhylomeDBi | P05459 |
Enzyme and pathway databases
UniPathwayi | UPA00244;UER00310 |
BioCyci | EcoCyc:ERYTHRON4PDEHYDROG-MONOMER |
BRENDAi | 1.1.1.290, 2026 |
Miscellaneous databases
PROi | PR:P05459 |
Family and domain databases
CDDi | cd12158, ErythrP_dh, 1 hit |
Gene3Di | 3.30.1370.170, 1 hit |
HAMAPi | MF_01825, PdxB, 1 hit |
InterProi | View protein in InterPro IPR006139, D-isomer_2_OHA_DH_cat_dom IPR029753, D-isomer_DH_CS IPR029752, D-isomer_DH_CS1 IPR006140, D-isomer_DH_NAD-bd IPR020921, Erythronate-4-P_DHase IPR024531, Erythronate-4-P_DHase_dimer IPR036291, NAD(P)-bd_dom_sf IPR038251, PdxB_dimer_sf |
Pfami | View protein in Pfam PF00389, 2-Hacid_dh, 1 hit PF02826, 2-Hacid_dh_C, 1 hit PF11890, DUF3410, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00065, D_2_HYDROXYACID_DH_1, 1 hit PS00671, D_2_HYDROXYACID_DH_3, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PDXB_ECOLI | |
Accessioni | P05459Primary (citable) accession number: P05459 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1988 |
Last sequence update: | April 1, 1990 | |
Last modified: | February 23, 2022 | |
This is version 174 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
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families