Reviewed, UniProtKB/Swiss-Prot Q3YXU5 (E4PD_SHISS)

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:	SSON_3079

Organism

Shigella sonnei (strain Ss046) [Complete proteome] [HAMAP]

Taxonomic identifier

300269 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 339	338	D-erythrose-4-phosphate dehydrogenase		PRO_0000293172
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	81	1	NAD; via carbonyl oxygen 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)
	Q3YXU5-1 [UniParc]. Last modified September 27, 2005. Version 1. Checksum: 4CFC4BD2267EA2A2	FASTA	339	37,299
	10 20 30 40 50 60 MTVRVAINGF GRIGRNVVRA LYESGRRAEI TVVAINELAD AAGMAHLLKY DTSHGRFAWE 70 80 90 100 110 120 VRQERDQLFV GDDAIRVLHE RSLQSLPWRE LGVDVVLDCT GVYGSREHGE AHIAAGAKKV 130 140 150 160 170 180 LFSHPGSNDL DATVVYGVNQ DQLRAEHRIV SNASCTTNCI IPVIKLLDDA YGIESGTVTT 190 200 210 220 230 240 IHSAMHDQQV IDAYHPDLRR TRAASQSIIP VDTKLAAGIT RFFPQFNDRF EAIAVRVPTI 250 260 270 280 290 300 NVTAIDLSVT VKKPVKANEV NLLLQKAAQG AFHGIVDYTE LPLVSVDFNH DPHSAIVDGT 310 320 330 QTRVSGAHLI KTLVWCDNEW GFANRMLDTT LAMATVAFR

References

[1]

"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery." Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q. Nucleic Acids Res. 33:6445-6458(2005) [PubMed: 16275786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000038 Genomic DNA. Translation: AAZ89667.1.
RefSeq	YP_311902.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3669214.
GenomeReviews	Gene locus SSON_3079 in contig CP000038_GR.
KEGG	ssn:SSON_3079.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q3YXU5.
Enzyme and pathway databases
BioCyc	SSON300269:SSO_3079-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_SHISS

Accession

Primary (citable) accession number: Q3YXU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	September 27, 2005
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)