Reviewed, UniProtKB/Swiss-Prot Q8EIB2 (E4PD_SHEON)

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:	SO_0931

Organism

Shewanella oneidensis [Complete proteome] [HAMAP]

Taxonomic identifier

70863 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

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+ + 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.
Subcellular location	Cytoplasm By 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: 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_0000293164
Regions
	Nucleotide binding	11 – 12	2	NAD By similarity
	Region	153 – 155	3	Substrate binding Potential
	Region	212 – 213	2	Substrate binding Potential
Sites
	Active site	154	1	Nucleophile By similarity
	Binding site	199	1	Substrate Potential
	Binding site	235	1	Substrate Potential
	Binding site	317	1	NAD By similarity
	Site	181	1	Activates thiol group during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8EIB2-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: FB58AA57643E8006	FASTA	338	37,241
	10 20 30 40 50 60 MIRVAINGYG RIGRSILRAL YESGKRQQIQ IVAINELAKP EAIIHLTQYD TTHGRFQPRV 70 80 90 100 110 120 KLVDGQMQIG DDTIKIFHEP DPAKLPWREL DIDIVYEATG AILDRQSCEA HIHAGAKQVL 130 140 150 160 170 180 ISHPSSADVD GTIVYGVNHD LLRAEHTVVS NASCTTNCIV PVIDVLDKHF GVKSGAITTI 190 200 210 220 230 240 HSAMNDQQVI DAYHDDLRRT RAAGQSIIPV DTKLARGIER ILPHMKDKFE AISVRVPTIN 250 260 270 280 290 300 VTAIDLSVTL DKTVDIATVN QVLELAANGR FNGILGYTDE PLVSCDFNHD PRSSIVDGTQ 310 320 330 TRVSAGQLVK LLLWCDNEWG FANRMLDTSL AMIAAKQS

References

[1]

"Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis." Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T. , Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., Nealson K.H., Fraser C.M. Nat. Biotechnol. 20:1118-1123(2002) [PubMed: 12368813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MR-1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014299 Genomic DNA. Translation: AAN54005.1.
RefSeq	NP_716560.1.
3D structure databases
HSSP	HSSP built from PDB template 1DBV based on UniProtKB P00362.
ModBase	Search...
Genome annotation databases
GeneID	1168777.
GenomeReviews	Gene locus SO_0931 in contig AE014299_GR.
KEGG	son:SO_0931.
NMPDR	fig|211586.1.peg.868.
TIGR	SO_0931.
Phylogenomic databases
HOGENOM	Q8EIB2.
OMA	Q8EIB2. AMDLSVT.
Enzyme and pathway databases
BioCyc	SONE211586:SO_0931-MON.
BRENDA	1.2.1.72. 257422.
Family and domain databases
HAMAP	MF_01640. [Tree]
InterPro	IPR006422. E4P_DH_bac. IPR000173. GlycerAld_3-P_DH. [Graphical view]
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_SHEON

Accession

Primary (citable) accession number: Q8EIB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 50 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)