Q6D086 (E4PD_ERWCT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-erythrose-4-phosphate dehydrogenase
Short name=E4PDH
EC=1.2.1.72

Gene names

Name:	epd
Ordered Locus Names:	ECA3913

Organism

Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]

Taxonomic identifier

29471 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Pyridoxine biosynthesis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: InterPro pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 338	338	D-erythrose-4-phosphate dehydrogenase HAMAP MF_01640		PRO_0000293149
Regions
	Nucleotide binding	12 – 13	2	NAD By similarity
	Region	154 – 156	3	Substrate binding Potential
	Region	213 – 214	2	Substrate binding Potential
Sites
	Active site	155	1	Nucleophile By similarity
	Binding site	200	1	Substrate Potential
	Binding site	236	1	Substrate Potential
	Binding site	318	1	NAD By similarity
	Site	182	1	Activates thiol group during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6D086 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: C0E3B6F822589F75	FASTA	338	37,303
	10 20 30 40 50 60 MTIRIAINGF GRIGRSVLRA LYESGRRAEI TVVAINELAS AEGMAHLLKY DSSHGRFSWD 70 80 90 100 110 120 VRQECDQLYV GDDDIRLLHQ VEIQQLPWRE LSVDIVLDCS GVYGSREDGE AHLAAGAKKV 130 140 150 160 170 180 LFSHPGTTDL DATVVFGVNH DRLESGHRIV SNASCTTNCI IPVIKLLDDA FGIENGTVTT 190 200 210 220 230 240 IHSSMNDQPV IDAYHHDLRR TRAASQSIIP VDTKLSAGIT RIFPQFVDRF EAISVRVPTI 250 260 270 280 290 300 NVTAIDLSVS VRKAVNVNEI NALLQKSAHE SFRGIVDYTE LPLVSADFNH DPHSAIVDGT 310 320 330 QTRVSGQHLI KTLVWCDNEW GFANRMLDTT RAMAACGF

References

[1]

"Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors." Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z. , Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K. Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004) [PubMed: 15263089] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SCRI 1043 / ATCC BAA-672.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX950851 Genomic DNA. Translation: CAG76811.1.
RefSeq	YP_052001.1. NC_004547.2.
3D structure databases
HSSP	HSSP built from PDB template 1S7C based on UniProtKB P0A9B2.
ProteinModelPortal	Q6D086.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2884534.
GenomeReviews	Gene locus ECA3913 in contig BX950851_GR.
KEGG	eca:ECA3913.
NMPDR	fig|218491.3.peg.2557.
PATRIC	20483245. VBIPecAtr54885_3976.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG571736.
OMA	TTHGRFQ.
ProtClustDB	PRK13535.
Enzyme and pathway databases
BioCyc	ECAR218491:ECA3913-MONOMER.
Family and domain databases
HAMAP	MF_01640. E4P_dehydrog. [Tree]
InterPro	IPR006422. 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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K03472.
PANTHER	PTHR10836. GAP_DH. 1 hit. PTHR10836:SF24. PTHR10836:SF24. 1 hit.
Pfam	PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000149. GAP_DH. 1 hit.
PRINTS	PR00078. G3PDHDRGNASE.
SMART	SM00846. Gp_dh_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01532. E4PD_g-proteo. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

E4PD_ERWCT

Accession

Primary (citable) accession number: Q6D086

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program