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Protein

Erythronate-4-phosphate dehydrogenase

Gene

pdxB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.UniRule annotation

Catalytic activityi

4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH.UniRule annotation

Pathwayi: pyridoxine 5'-phosphate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate.UniRule annotation1 Publication
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. D-erythrose-4-phosphate dehydrogenase (epd)
  2. Erythronate-4-phosphate dehydrogenase (pdxB)
  3. Phosphoserine aminotransferase (serC)
  4. 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA)
  5. Pyridoxine 5'-phosphate synthase (pdxJ)
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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei45SubstrateUniRule annotation1
Binding sitei66SubstrateUniRule annotation1
Binding sitei146NADUniRule annotation1
Binding sitei175NAD; via carbonyl oxygenUniRule annotation1
Active sitei208UniRule annotation1
Binding sitei232NADUniRule annotation1
Active sitei237UniRule annotation1
Active sitei254Proton donorUniRule annotation1
Binding sitei257NAD; via amide nitrogenUniRule annotation1
Binding sitei258SubstrateUniRule annotation1

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 functionOxidoreductase
Biological processPyridoxine biosynthesis
LigandNAD

Enzyme and pathway databases

BioCyciEcoCyc:ERYTHRON4PDEHYDROG-MONOMER
MetaCyc:ERYTHRON4PDEHYDROG-MONOMER
BRENDAi1.1.1.290 2026
UniPathwayiUPA00244; 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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10692 pdxB

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000759751 – 378Erythronate-4-phosphate dehydrogenaseAdd BLAST378

Proteomic databases

EPDiP05459
PaxDbiP05459
PRIDEiP05459

Expressioni

Inductioni

During growth rate.1 Publication

Interactioni

Subunit structurei

Homodimer.UniRule annotation

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4259616, 24 interactors
DIPiDIP-10449N
IntActiP05459, 9 interactors
STRINGi316385.ECDH10B_2482

Structurei

3D structure databases

ProteinModelPortaliP05459
SMRiP05459
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CJ0 Bacteria
COG0111 LUCA
HOGENOMiHOG000234432
InParanoidiP05459
KOiK03473
OMAiSAPGCNA
PhylomeDBiP05459

Family and domain databases

CDDicd12158 ErythrP_dh, 1 hit
Gene3Di3.30.1370.170, 1 hit
HAMAPiMF_01825 PdxB, 1 hit
InterProiView 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
PANTHERiPTHR42938:SF3 PTHR42938:SF3, 1 hit
PfamiView protein in Pfam
PF00389 2-Hacid_dh, 1 hit
PF02826 2-Hacid_dh_C, 1 hit
PF11890 DUF3410, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00065 D_2_HYDROXYACID_DH_1, 1 hit
PS00671 D_2_HYDROXYACID_DH_3, 1 hit

Sequencei

Sequence statusi: Complete.

P05459-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:378
Mass (Da):41,368
Last modified:April 1, 1990 - v2
Checksum:i6CEF17691CF2C14A
GO

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
PIRiJV0051 DEECPP
RefSeqiNP_416823.1, NC_000913.3
WP_000699148.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75380; AAC75380; b2320
BAA16177; BAA16177; BAA16177
GeneIDi946785
KEGGiecj:JW2317
eco:b2320
PATRICifig|1411691.4.peg.4413

Similar proteinsi

Entry informationi

Entry nameiPDXB_ECOLI
AccessioniPrimary (citable) accession number: P05459
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: April 1, 1990
Last modified: March 28, 2018
This is version 158 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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