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A1JPR1 (E4PD_YERE8) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-erythrose-4-phosphate dehydrogenase

Short name=E4PDH
EC=1.2.1.72
Gene names
Name:epd
Ordered Locus Names:YE3415
OrganismYersinia enterocolitica serotype O:8 / biotype 1B (strain 8081) [Complete proteome] [HAMAP]
Taxonomic identifier393305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate By similarity. HAMAP MF_01640

Catalytic activity

D-erythrose 4-phosphate + NAD+ + H2O = 4-phosphoerythronate + NADH. HAMAP MF_01640

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 1/5. HAMAP MF_01640

Subunit structure

Homotetramer By similarity. HAMAP MF_01640

Subcellular location

Cytoplasm By similarity HAMAP MF_01640.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. Epd subfamily.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpyridoxal phosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

pyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

erythrose-4-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338D-erythrose-4-phosphate dehydrogenase HAMAP MF_01640
PRO_0000293178

Regions

Nucleotide binding12 – 132NAD By similarity
Region154 – 1563Substrate binding Potential
Region213 – 2142Substrate binding Potential

Sites

Active site1551Nucleophile By similarity
Binding site2001Substrate Potential
Binding site2361Substrate Potential
Binding site3181NAD By similarity
Site1821Activates thiol group during catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
A1JPR1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: D4D3E2DF8E0237D0

FASTA33837,075
        10         20         30         40         50         60 
MTIRIAINGF GRIGRSVLRA LYESGRRAEI SVVAINELAN AEGMAHLLKY DSSHGRFAWD 

        70         80         90        100        110        120 
VRQECDKLYV GDDIIRLIHQ PEIEQLPWGE LGIDVVLDCS GVYGSRADGE AHLTSGAKKV 

       130        140        150        160        170        180 
LFAHPGGHDL DATVVYGVNH QDLQADHRIV SNASCTTNCI IPIIQLLDVA FGIESGTVTT 

       190        200        210        220        230        240 
IHSSMNDQPV IDAYHQDLRR TRAASQSIIP VDTKLAAGIT RIFPKFCDRF EAISVRVPTI 

       250        260        270        280        290        300 
NVTAIDLSVS VTSPVDVAEV NQLLQKAARG SFRGIVDYTE LPLVSTDFNH DPHSAIVDCT 

       310        320        330 
QTRVSGQHLI KTLVWCDNEW GFANRMLDTT LAMARSGF 

« Hide

References

[1]"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081."
Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. expand/collapse author list , Quail M.A., Dougan G., Parkhill J., Prentice M.B.
PLoS Genet. 2:2039-2051(2006) [PubMed: 17173484] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 8081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286415 Genomic DNA. Translation: CAL13439.1.
RefSeqYP_001007581.1. NC_008800.1.

3D structure databases

ProteinModelPortalA1JPR1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1JPR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4713807.
GenomeReviewsGene locus YE3415 in contig AM286415_GR.
KEGGyen:YE3415.
NMPDRfig|630.2.peg.3340.
PATRIC18566585. VBIYerEnt11519_3626.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0057.
HOGENOMHBG571736.
OMATTHGRFQ.
PhylomeDBA1JPR1.
ProtClustDBPRK13535.

Enzyme and pathway databases

BioCycYENT393305:YE3415-MONOMER.

Family and domain databases

HAMAPMF_01640. E4P_dehydrog.
[Tree]
InterProIPR006422. E4P_DH_bac.
IPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK03472.
PANTHERPTHR10836. GAP_DH. 1 hit.
PTHR10836:SF24. PTHR10836:SF24. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01532. E4PD_g-proteo. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE4PD_YERE8
AccessionPrimary (citable) accession number: A1JPR1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families