Reviewed, UniProtKB/Swiss-Prot Q6LMN0 (E4PD_PHOPR)

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:	PBPRA3132

Organism

Photobacterium profundum (Photobacterium sp. (strain SS9)) [Complete proteome] [HAMAP]

Taxonomic identifier

74109 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Photobacterium

Protein attributes

Sequence length	360 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(+) + H(2)O = 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	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
	Chain	1 – 360	360	D-erythrose-4-phosphate dehydrogenase HAMAP MF_01640		PRO_0000293152
Regions
	Nucleotide binding	12 – 13	2	NAD By similarity
	Region	159 – 161	3	Substrate binding Potential
	Region	218 – 219	2	Substrate binding Potential
Sites
	Active site	160	1	Nucleophile By similarity
	Binding site	205	1	Substrate Potential
	Binding site	241	1	Substrate Potential
	Binding site	323	1	NAD By similarity
	Site	187	1	Activates thiol group during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6LMN0-1 [UniParc]. Last modified July 10, 2007. Version 2. Checksum: 71F1F3068FD89B04	FASTA	360	39,834
	10 20 30 40 50 60 MTLKVAINGF GRIGRSVLRA LYESGKHHHI NVVAVNELAE PEAMAHLLQY DSSHGRFFKP 70 80 90 100 110 120 VSHDQEHLFI AHENGERDDI RILHQSDITL LPWHDLDVDI VLDCTGVYGS REDGLAHIKA 130 140 150 160 170 180 GAKKVLFSHP AANDIDNTII YGVNHKTLTS EHRIVSNGSC TTNCIVPVIK IIDDAFGIES 190 200 210 220 230 240 GTITTIHSAM NDQQVIDGYH SDLRRTRAAS QSIIPVDTKL HLGIGRIFPK FVDKFEAISV 250 260 270 280 290 300 RVPTINVTAM DLSVTVKTNV KVNDVNQALS EVSRCTLEGI VDYTEAPLVS IDFNHDPHSA 310 320 330 340 350 360 IVDGTQTRVS NKHLIKLLVW CDNEWGFANR MLDTALAMHA SDAAQHSNKE LRSKIAIKNS

References

[1]

"Life at depth: Photobacterium profundum genome sequence and expression analysis." Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., Bartlett D.H., Valle G. Science 307:1459-1461(2005) [PubMed: 15746425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR378673 Genomic DNA. Translation: CAG21447.1. Different initiation.
RefSeq	YP_131249.2.
3D structure databases
HSSP	HSSP built from PDB template 1DC5 based on UniProtKB P06977.
ModBase	Search...
Genome annotation databases
GeneID	3123661.
GenomeReviews	Gene locus PBPRA3132 in contig CR354531_GR.
KEGG	ppr:PBPRA3132.
NMPDR	fig|298386.1.peg.5356.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6LMN0.
Enzyme and pathway databases
BioCyc	PPRO298386:PBPRA3132-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. 2 hits.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

E4PD_PHOPR

Accession

Primary (citable) accession number: Q6LMN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	July 10, 2007
Last modified:	November 25, 2008
This is version 32 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)