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A4SRF2 (E4PD_AERS4) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 38. 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:ASA_3506
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length336 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 – 336336D-erythrose-4-phosphate dehydrogenase HAMAP MF_01640
PRO_0000293144

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
A4SRF2 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: E8921487B5FB191C

FASTA33636,786
        10         20         30         40         50         60 
MIKIAINGYG RIGRNVLRAL YESGRDKNIK IVAINELAAP EAMVHLTRFD TSHGRFRYPV 

        70         80         90        100        110        120 
QLAGHSMLVG EDLISLFAEQ DPANLPWRAL GVDVVLDCTG VFGSRADAEL HLGAGAGKVL 

       130        140        150        160        170        180 
FSHPADADVD ATIVYGVNHQ VLTGRERIVS NASCTTNCVV PVIETLHREF EINCGTITTI 

       190        200        210        220        230        240 
HSAMHDQQVI DAYHSDLRRT RAASQSIIPV DTKLAKGLER ILPHFAGKFE AIAVRVPTIN 

       250        260        270        280        290        300 
VTAMDLSITV RKKVTVTDVN QALQRASRGT LSGILDYTEE PLVSVDFNHD AHSCIIDGTQ 

       310        320        330 
TRVSDANLVK MLMWCDNEWG FANRMLDTTR AMMAAG 

« Hide

References

[1]"The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
BMC Genomics 9:427-427(2008) [PubMed: 18801193] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A449.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000644 Genomic DNA. Translation: ABO91474.1.
RefSeqYP_001143222.1. NC_009348.1.

3D structure databases

ProteinModelPortalA4SRF2.
SMRA4SRF2. Positions 2-335.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4SRF2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4997757.
GenomeReviewsGene locus ASA_3506 in contig CP000644_GR.
KEGGasa:ASA_3506.
PATRIC20793468. VBIAerSal2987_3494.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0057.
HOGENOMHBG571736.
OMATTHGRFQ.
PhylomeDBA4SRF2.
ProtClustDBPRK13535.

Enzyme and pathway databases

BioCycASAL382245:ASA_3506-MONOMER.

Family and domain databases

HAMAPMF_01640. E4P_dehydrog.
[Tree]
InterProIPR006422. E4P_DH_bac.
IPR020831. GlycerAld/Erythrose_P_DH.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE4PD_AERS4
AccessionPrimary (citable) accession number: A4SRF2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: May 15, 2007
Last modified: December 14, 2011
This is version 38 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