Reviewed, UniProtKB/Swiss-Prot Q666Q0 (E4PD_YERPS)

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:	YPTB3197

Organism

Yersinia pseudotuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

633 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Pyridoxine biosynthesis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP pyridoxine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro erythrose-4-phosphate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity Inferred from electronic annotation. Source: InterPro
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		PRO_0000293182
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)
	Q666Q0-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 5E0A54DCAD224E06	FASTA	338	37,015
	10 20 30 40 50 60 MAIRIAINGF GRIGRSVLRA LYESGRRAEI SVVAINELAS AEGMAHLLKY DSSHGRFAWD 70 80 90 100 110 120 VRQECDSLYV GDDIIRLIHQ SEIEQLPWSE LGIDVVLDCS GVYGSREDGE AHVASGAKKV 130 140 150 160 170 180 LFAHPGGHDL DATVVYGVNH QDLRAEHRIV SNASCTTNCI IPIIQLLDIA YGIESGTVTT 190 200 210 220 230 240 IHSSMNDQPV IDAYHQDLRR TRAASQSIIP VDTKLAAGIT RIFPKFCDRF EAISVRVPTI 250 260 270 280 290 300 NVTAIDLSVS VTHPVGVAEV NQLLQKAARG AFRGIVDYTE LPLVSMDFNH DPHSAIVDGT 310 320 330 QTRVSGQHLI KTLVWCDNEW GFANRMLDTT LAMAKSGF

References

[1]

"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis." Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E. Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed: 15358858] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IP32953 / Serotype I.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX936398 Genomic DNA. Translation: CAH22435.1.
RefSeq	YP_071698.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2955509.
GenomeReviews	Gene locus YPTB3197 in contig BX936398_GR.
KEGG	yps:YPTB3197.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q666Q0.
Enzyme and pathway databases
BioCyc	YPSE273123:YPTB3197-MON.
Family and domain databases
HAMAP	MF_01640. [Tree]
InterPro	IPR006422. E4P_DHase_bac. IPR000173. GlycerAld_3-P_DHase. IPR016040. NAD(P)-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR10836. GAP_DH. 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.
TIGRFAMs	TIGR01532. E4PD_g-proteo. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

E4PD_YERPS

Accession

Primary (citable) accession number: Q666Q0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	October 11, 2004
Last modified:	November 25, 2008
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)