Reviewed, UniProtKB/Swiss-Prot Q5PJI5 (E4PD_SALPA)

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:	SPA2941

Organism

Salmonella paratyphi A [Complete proteome] [HAMAP]

Taxonomic identifier

54388 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	348 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 – 348	348	D-erythrose-4-phosphate dehydrogenase HAMAP MF_01640		PRO_0000293157
Regions
	Nucleotide binding	12 – 13	2	NAD By similarity
	Region	154 – 156	3	Substrate binding Potential
	Region	213 – 214	2	Substrate binding Potential
Sites
	Active site	155	1	Nucleophile By similarity
	Binding site	81	1	NAD; via carbonyl oxygen By similarity
	Binding site	200	1	Substrate Potential
	Binding site	236	1	Substrate Potential
	Binding site	318	1	NAD By similarity
	Site	182	1	Activates thiol group during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PJI5-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: ABA3407EE0B21857	FASTA	348	38,125
	10 20 30 40 50 60 MTVRIAINGF GRIGRNVVRA LYESGRRAEI TVVAINELAD AAGMAHLLKY DTSHGRFAWE 70 80 90 100 110 120 VRHEREQLFV GDDVIRILHE RTLADLPWRE LGVDVVLDCT GVYGNQEHGE AHIAAGAKKV 130 140 150 160 170 180 LFSHPGSNDL DATVVFGVNQ NQLRAEHRIV SNASCTTNCI IPVIKLLDDA YGIESGTVTA 190 200 210 220 230 240 IHSAMNDQQV IDAYHSDLRR TRAASQSIIP VDTKLAAGIT RIFPQFNDRF EAIAVRVPTI 250 260 270 280 290 300 NVTAIDLSVT VKKPVKASEV NQLLQKAAQG AFHGIVDYTE SPLVSIDFNH DPHSAIVDGT 310 320 330 340 QTRVSGAHLI KTLVWCDNEW GFANRMLDTT LAMAAVDFRL DASASTKL

References

[1]

"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid." McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K. Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000026 Genomic DNA. Translation: AAV78779.1.
RefSeq	YP_152091.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3177549.
GenomeReviews	Gene locus SPA2941 in contig CP000026_GR.
KEGG	spt:SPA2941.
NMPDR	fig|295319.3.peg.2820.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5PJI5.
OMA	Q5PJI5. AMDLSVT.
Enzyme and pathway databases
BioCyc	SENT295319:SPA2941-MON.
Family and domain databases
HAMAP	MF_01640. [Tree]
InterPro	IPR006422. E4P_DH_bac. IPR000173. GlycerAld_3-P_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
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_SALPA

Accession

Primary (citable) accession number: Q5PJI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	January 4, 2005
Last modified:	June 16, 2009
This is version 32 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)