Reviewed, UniProtKB/Swiss-Prot Q0HRM3 (E4PD_SHESR)

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:	Shewmr7_3249

Organism

Shewanella sp. (strain MR-7) [Complete proteome] [HAMAP]

Taxonomic identifier

60481 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

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_0000293167
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)
	Q0HRM3-1 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: 792397BC6A173702	FASTA	338	37,229
	10 20 30 40 50 60 MIRVAINGYG RIGRSILRAL YESGKRQQIQ IVAINELAKP EAIVHLTQYD TTHGRFQPRV 70 80 90 100 110 120 KLVDDQMLIG DDVIKILHEP DPAKLPWREM DIDIVYEATG AILDRNSCEA HIHAGAKQVL 130 140 150 160 170 180 ISHPSSADVD GTIVYGVNQD 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]

"Complete sequence of chromosome 1 of Shewanella sp. MR-7." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., Tiedje J., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000444 Genomic DNA. Translation: ABI44232.1.
RefSeq	YP_739289.1.
3D structure databases
SMR	Q0HRM3. Positions 2-332.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0HRM3.
Genome annotation databases
GeneID	4256941.
GenomeReviews	Gene locus Shewmr7_3249 in contig CP000444_GR.
KEGG	shm:Shewmr7_3249.
NMPDR	fig|60481.10.peg.3063.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0057.
HOGENOM	HBG571736.
OMA	IQAKAVR.
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]
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_SHESR

Accession

Primary (citable) accession number: Q0HRM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	October 3, 2006
Last modified:	February 9, 2010
This is version 29 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)