Skip Header

Contribute Send feedback
Read comments (?) or add your own

A1S9A4 (E4PD_SHEAM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:Sama_2758
OrganismShewanella amazonensis (strain ATCC BAA-1098 / SB2B) [Complete proteome] [HAMAP]
Taxonomic identifier326297 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

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_0000293160

Regions

Nucleotide binding11 – 122NAD By similarity
Region153 – 1553Substrate binding Potential
Region212 – 2132Substrate binding Potential

Sites

Active site1541Nucleophile By similarity
Binding site1991Substrate Potential
Binding site2351Substrate Potential
Binding site3171NAD By similarity
Site1811Activates thiol group during catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
A1S9A4 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 6763094EDDB58655

FASTA33836,429
        10         20         30         40         50         60 
MIRVAINGYG RIGRSVLRAL YESGKRGQMQ LVAINELAKP EAIVHLTNYD TTHGRFHTRA 

        70         80         90        100        110        120 
SLDEGMMHLG NDAIRLLAIE DAAALPWQAL DVDLVFECTG ALNDRQSAEA HITAGARKVL 

       130        140        150        160        170        180 
ISHPSSADVD ATIVYGVNDA SLKATDTVVS NASCTTNCLV PVIDVLDRHF GVKSGAITTI 

       190        200        210        220        230        240 
HSAMNDQQVI DAYHDDLRRT RAASQSIIPV DTKLARGIER ILPQMKDKFE AISVRVPTIN 

       250        260        270        280        290        300 
VTAIDLSVTL DTRVDIATVN AALKAAADGS ASGILGYTDE PLVSCDFNHD PRSSVVDGTQ 

       310        320        330 
TRVSAGHLVK MLLWCDNEWG FANRMLDTAL AMAATQAE 

« Hide

References

[1]"Complete sequence of Shewanella amazonensis SB2B."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1098 / SB2B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000507 Genomic DNA. Translation: ABM00961.1.
RefSeqYP_928630.1. NC_008700.1.

3D structure databases

ProteinModelPortalA1S9A4.
SMRA1S9A4. Positions 2-335.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1S9A4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4605005.
GenomeReviewsGene locus Sama_2758 in contig CP000507_GR.
KEGGsaz:Sama_2758.
NMPDRfig|326297.7.peg.2585.
PATRIC23454363. VBISheAma74963_2833.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0057.
HOGENOMHBG571736.
OMATTHGRFQ.
PhylomeDBA1S9A4.
ProtClustDBPRK13535.

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.
KOK00134.
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_SHEAM
AccessionPrimary (citable) accession number: A1S9A4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 43 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