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Reviewed, UniProtKB/Swiss-Prot Q7N7Z6 (E4PD_PHOLL)

Last modified November 25, 2008. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: plu0955
OrganismPhotorhabdus luminescens subsp. laumondii [Complete proteome] [HAMAP]
Taxonomic identifier141679 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

D-erythrose 4-phosphate + NAD(+) + H(2)O = 4-phosphoerythronate + NADH.

Pathway

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

Subunit structure

Homotetramer By similarity.

Subcellular location

CytoplasmBy similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339D-erythrose-4-phosphate dehydrogenase
PRO_0000293151

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
Q7N7Z6-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: FC7709CF577F7B96

FASTA33937,149
        10         20         30         40         50         60 
MTIKVAINGF GRIGRSILRA LYESGRRAEI AVIAVNELAD AEGIAHLLKY DSSHGRFAWD 

        70         80         90        100        110        120 
VRLNNDVLQV GDDNIRLFHQ SDISMLPWQE LGIDIVLDCS GIYGSRADGE AHLASGAKKV 

       130        140        150        160        170        180 
LFAHPGGNDL DATVVYGVNQ HLLTAEDRIV SNASCTTNCI IPIIKLLDDQ FEIESGTVTT 

       190        200        210        220        230        240 
IHASMNDQPV IDAYHKDLRR TRAASQSIIP VDTKLAAGIT RIFPKFCDRF EAISVRVPTI 

       250        260        270        280        290        300 
NVTAIDLSVT VKSSVTVNKI NELMQKSAAT SFRGIVDYTE LPLVSTDFNH DPHSAIVDGT 

       310        320        330 
QTRVSGQHLI KTLVWCDNEW GFANRMLDTT LAMAAMGFK 

« Hide

Cross-references

Sequence databases

BX571862 Genomic DNA. Translation: CAE13250.1.
RefSeqNP_928289.1.

3D structure databases

HSSPHSSP built from PDB template 1HDG based on UniProtKB P17721.
ModBaseSearch...

Genome annotation databases

GeneID2800919.
GenomeReviewsGene locus plu0955 in contig BX470251_GR.
KEGGplu:plu0955.
NMPDRfig|243265.1.peg.913.

Organism-specific databases

PhotoListplu0955.
CMRSearch...

Phylogenomic databases

HOGENOMQ7N7Z6.

Enzyme and pathway databases

BioCycPLUM243265:PLU0955-MON.

Family and domain databases

HAMAPMF_01640.
[Tree]
InterProIPR006422. E4P_DHase_bac.
IPR000173. GlycerAld_3-P_DHase.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR10836. GAP_DH. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
TIGRFAMsTIGR01532. E4PD_g-proteo. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE4PD_PHOLL
AccessionPrimary (citable) accession number: Q7N7Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: December 15, 2003
Last modified: November 25, 2008
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents