Reviewed, UniProtKB/Swiss-Prot A0KGD2 (E4PD_AERHH)

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:	AHA_0780

Organism

Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]

Taxonomic identifier

380703 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length	336 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 – 336	336	D-erythrose-4-phosphate dehydrogenase HAMAP MF_01640		PRO_0000293143
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	80	1	NAD; via carbonyl oxygen 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)
	A0KGD2-1 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: D799CCDE4474D1ED	FASTA	336	36,832
	10 20 30 40 50 60 MIKIAINGYG RIGRNVLRAL YESGRDKNIK IVAINELAAP EAMVHLTRFD TSHGRFHHPV 70 80 90 100 110 120 QLAGNSMLVG EDLISLFAER DPSRLPWRAL GVDVVLDCTG VFGSRADAEL HLAAGAGKVL 130 140 150 160 170 180 FSHPAEADVD ATIVYGVNHQ VLTGRERIVS NASCTTNCVV PVIETLHREF EINCGTITTI 190 200 210 220 230 240 HSAMHDQQVI DAYHSDLRRT RAASQSIIPV DTKLAKGLER ILPHFAGKFE AIAVRVPTIN 250 260 270 280 290 300 VTAMDLSITV RKKVTVTDVN QALQRASRGT LSGILDYTEE PLVSVDFNHD AHSCIIDGTQ 310 320 330 TRVSDANLVK MLMWCDNEWG FANRMLDTTR AMMAAG

References

[1]

"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades." Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F. J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000462 Genomic DNA. Translation: ABK36491.1.
RefSeq	YP_855322.1.
3D structure databases
SMR	A0KGD2. Positions 2-335.
ModBase	Search...
Protein-protein interaction databases
STRING	A0KGD2.
Genome annotation databases
GeneID	4487940.
GenomeReviews	Gene locus AHA_0780 in contig CP000462_GR.
KEGG	aha:AHA_0780.
TIGR	AHA_0780.
Phylogenomic databases
eggNOG	COG0057.
HOGENOM	HBG571736.
OMA	IQAKAVR.
PhylomeDB	A0KGD2.
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]
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.
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_AERHH

Accession

Primary (citable) accession number: A0KGD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	December 12, 2006
Last modified:	February 9, 2010
This is version 27 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)