Reviewed, UniProtKB/Swiss-Prot Q1CEY2 (E4PD_YERPN)

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:	YPN_3121
ORF Names:	YP516_3543

Organism

Yersinia pestis bv. Antiqua (strain Nepal516) [Complete proteome] [HAMAP]

Taxonomic identifier

377628 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

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	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: UniProtKB-SubCell
Molecular function	NAD or NADH 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 HAMAP MF_01640		PRO_0000293181
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)
	Q1CEY2-1 [UniParc]. Last modified July 11, 2006. 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]	"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen." Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L. J. Bacteriol. 188:4453-4463(2006) [PubMed: 16740952] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Yersinia pestis Nepal516A whole genome shotgun sequencing project." Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L., Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R., Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S. Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000305 Genomic DNA. Translation: ABG19448.1. ACNQ01000017 Genomic DNA. Translation: EEO75613.1.
RefSeq	YP_649048.1.
3D structure databases
SMR	Q1CEY2. Positions 2-336.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1CEY2.
Genome annotation databases
GeneID	4123800.
GenomeReviews	Gene locus YPN_3121 in contig CP000305_GR.
KEGG	ypn:YPN_3121.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0057.
HOGENOM	HBG571736.
OMA	IQAKAVR.
Enzyme and pathway databases
BioCyc	YPES377628:YPN_3121-MONOMER.
Family and domain databases
HAMAP	MF_01640. E4P_dehydrog. [Tree]
InterPro	IPR006422. E4P_DH_bac. IPR020830. GlycerAld_3-P_DH_AS. IPR020829. GlycerAld_3-P_DH_cat. IPR020832. GlycerAld_3-P_DH_cat_sub. IPR020831. GlycerAld_3-P_DH_family. IPR020828. GlycerAld_3-P_DH_NAD(P)_bd. IPR000173. GlycerAld_3-P_DH_subfam. IPR016040. NAD(P)-bd_dom. [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.
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_YERPN

Accession

Primary (citable) accession number: Q1CEY2
Secondary accession number(s): C4GXG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	July 11, 2006
Last modified:	February 9, 2010
This is version 32 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)