Reviewed, UniProtKB/Swiss-Prot Q5QVL6 (E4PD_IDILO)

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:	IL2213

Organism

Idiomarina loihiensis [Complete proteome] [HAMAP]

Taxonomic identifier

135577 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina

Protein attributes

Sequence length	341 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 – 341	341	D-erythrose-4-phosphate dehydrogenase HAMAP MF_01640		PRO_0000293150
Regions
	Nucleotide binding	14 – 15	2	NAD By similarity
	Region	156 – 158	3	Substrate binding Potential
	Region	215 – 216	2	Substrate binding Potential
Sites
	Active site	157	1	Nucleophile By similarity
	Binding site	202	1	Substrate Potential
	Binding site	238	1	Substrate Potential
	Binding site	320	1	NAD By similarity
	Site	184	1	Activates thiol group during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5QVL6-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 5E307654A8D8D1B8	FASTA	341	37,680
	10 20 30 40 50 60 MSEPARIAIN GFGRIGRSFL RALYENGYRD SVQVVLINEP AASEAIAHLL KYDSSHGRFG 70 80 90 100 110 120 EKVTQSGDAL TVAGDNIALT HQTEIEAIDW RAHEVDFVVD CTGVFGSQAD GQLYLQQGVK 130 140 150 160 170 180 RVLFSHPGKP DVDFTAIYGV NEKELTVDHK VVSNGSCTTN CIVPVIKVLD DAFGIDSGAI 190 200 210 220 230 240 TTIHSAMHDQ QVIDAYHPDL RRTRAAGRSI IPVDTRLARG IERILPHLEG RFEAIAVRVP 250 260 270 280 290 300 TTNVTAMDLS VTLNSDATIE QINQVLREQS ERQLAGILDY TEEPLVSIDF NHDPHSSIVD 310 320 330 340 GTQTRVSHKR LVKLLCWCDN EWGFANRLLD TAKTMAEQTE H

References

[1]

"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy." Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. , Aizawa S., Shibata S., Malahoff A., Alam M. Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: L2-TR / ATCC BAA-735 / DSM 15497.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017340 Genomic DNA. Translation: AAV83045.1.
RefSeq	YP_156594.1.
3D structure databases
HSSP	HSSP built from PDB template 1GD1 based on UniProtKB P00362.
SMR	Q5QVL6. Positions 4-337.
ModBase	Search...
Genome annotation databases
GeneID	3174021.
GenomeReviews	Gene locus IL2213 in contig AE017340_GR.
KEGG	ilo:IL2213.
NMPDR	fig|283942.3.peg.2200.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG571736.
OMA	IQAKAVR.
Enzyme and pathway databases
BioCyc	ILOI283942:IL2213-MONOMER.
BRENDA	1.2.1.72. 280818.
Family and domain databases
HAMAP	MF_01640. E4P_dehydrog. [Tree]
InterPro	IPR006422. E4P_DH_bac. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

E4PD_IDILO

Accession

Primary (citable) accession number: Q5QVL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	January 4, 2005
Last modified:	February 9, 2010
This is version 40 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)