[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12 / CS520; DOI=10.1111/j.1365-2958.1989.tb00221.x; PubMed=2546007 [NCBI, ExPASy, EBI, Israel, Japan] Alefounder P.R., Perham R.N.; "Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli."; Mol. Microbiol. 3:723-732(1989).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[4]	PROTEIN SEQUENCE OF 2-13, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES. STRAIN=K12; PubMed=7751290 [NCBI, ExPASy, EBI, Israel, Japan] Zhao G., Pease A.J., Bharani N., Winkler M.E.; "Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis."; J. Bacteriol. 177:2804-2812(1995).
[5]	GENE TRANSFER DISCUSSION. DOI=10.1007/BF02106053; PubMed=2124629 [NCBI, ExPASy, EBI, Israel, Japan] Doolittle R.F., Feng D.F., Anderson K.L., Alberro M.R.; "A naturally occurring horizontal gene transfer from a eukaryote to a prokaryote."; J. Mol. Evol. 31:383-388(1990).
[6]	FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-155; HIS-182 AND CYS-316, MASS SPECTROMETRY, AND REACTION MECHANISM. DOI=10.1074/jbc.272.24.15106; PubMed=9182530 [NCBI, ExPASy, EBI, Israel, Japan] Boschi-Muller S., Azza S., Pollastro D., Corbier C., Branlant G.; "Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase."; J. Biol. Chem. 272:15106-15112(1997).
[7]	ROLE IN PNP BIOSYNTHESIS. PubMed=9696782 [NCBI, ExPASy, EBI, Israel, Japan] Yang Y., Zhao G., Man T.-K., Winkler M.E.; "Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12."; J. Bacteriol. 180:4294-4299(1998).

Comments

FUNCTION: Catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate.
CATALYTIC ACTIVITY: D-erythrose 4-phosphate + NAD⁺ + H₂O = 4-phosphoerythronate + NADH.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=74 µM for NAD (at 37 degrees Celsius and pH 8.6);
	K_M=510 µM for D-erythrose 4-phosphate (at 25 degrees Celsius and pH 8.9);
	K_M=960 µM for D-erythrose 4-phosphate (at 37 degrees Celsius and pH 8.6);
	K_M=1100 µM for glyceraldehyde 3-phosphate (at 25 degrees Celsius and pH 8.9);
	V_max=91.2 µmol/min/mg enzyme toward D-erythrose 4-phosphate (at 37 degrees Celsius and pH 8.6);
	V_max=77.2 µmol/min/mg enzyme toward NAD (at 37 degrees Celsius and pH 8.6);
pH dependence:	Optimum pH is about 8.6;
Temperature dependence:	Optimum temperature is 50 degrees Celsius at pH 8.6. Relatively thermostable. Activity begins to decrease significantly when E4PDH is incubated at 50 degrees Celsius for 5 min;

PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 1/5 .
SUBUNIT: Homotetramer.
INTERACTION:
P0A6F5:groL; NbExp=1; IntAct=EBI-1130931, EBI-543750;
SUBCELLULAR LOCATION: Cytoplasm.
MASS SPECTROMETRY: Mass=37170; Method=Unknown; Range=2-339; Source=PubMed:9182530;.
SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. Epd subfamily.
CAUTION: Was originally (PubMed:2546007 and PubMed:2124629) thought to be a glyceraldehyde 3-phosphate dehydrogenase, but glyceraldehyde 3-phosphate is not an efficient substrate (PubMed:7751290 and PubMed:9182530).

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X14436; CAA32603.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U28377; AAA69094.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75964.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76991.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S04732; DEECGB.

RefSeq

AP_003485.1; -.
NP_417402.1; -.

3D structure databases

HSSP

P00362; 1NQO. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

P0A9B6.

Protein-protein interaction databases

IntAct

P0A9B6; 1.

Enzyme and pathway databases

BioCyc

EcoCyc:ERYTH4PDEHYDROG-MON; -.
MetaCyc:ERYTH4PDEHYDROG-MON; -.

Organism-specific databases

EchoBASE

EB0363; -.

EcoGene

EG10368; epd.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0048001;	Molecular function: erythrose-4-phosphate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0004365;	Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from InterPro).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006006;	Biological process: glucose metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0042823;	Biological process: pyridoxal phosphate biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008615;	Biological process: pyridoxine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01640; -; 1.
PBIL [Tree]

InterPro

IPR006422; E4P_DHase_bac.
IPR000173; GlycerAld_3-P_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR10836; GAP_DH; 1.

Pfam

PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000149; GAP_DH; 1.

PRINTS

PR00078; G3PDHDRGNASE.

TIGRFAMs

TIGR01532; E4PD_g-proteo; 1.

PROSITE

PS00071; GAPDH; 1.

Genome annotation databases

GeneID

947413; -.

GenomeReviews

AP009048_GR; JW2894.
U00096_GR; b2927.

KEGG

ecj:JW2894; -.
eco:b2927; -.

Phylogenomic databases

HOGENOM

P0A9B6; -.

Genome annotation databases

CMR

P0A9B6; b2927.

Other

ProtoNet

P0A9B6.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Pyridoxine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 339`	`338`	`D-erythrose-4-phosphate dehydrogenase.`	`PRO_0000145650`
`NP_BIND`	`12 13`	`2`	`NAD (By similarity).`
`REGION`	`154 156`	`3`	`Substrate binding (Potential).`
`REGION`	`213 214`	`2`	`Substrate binding (Potential).`
`ACT_SITE`	`155 155`		`Nucleophile (By similarity).`
`BINDING`	`81 81`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`200 200`		`Substrate (Potential).`
`BINDING`	`236 236`		`Substrate (Potential).`
`BINDING`	`318 318`		`NAD (By similarity).`
`SITE`	`182 182`	`1`	`Activates thiol group during catalysis (By similarity).`
`MUTAGEN`	`155 155`		`C->A,G,V: No significant activity.`
`MUTAGEN`	`182 182`		`H->N: 10-fold reduction in activity. Increases affinity for D-erythrose-4-phosphate and reduces affinity for glyceraldehyde 3-phosphate.`
`MUTAGEN`	`316 316`		`C->A,Y: Reduces activity and affinity for D-erythrose-4-phosphate and increases affinity for glyceraldehyde 3-phosphate.`

Sequence information

Length: 339 AA [This is the length of the unprocessed precursor]

Molecular weight: 37299 Da [This is the MW of the unprocessed precursor]

CRC64: 4CFC4BD2267EA2A2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTVRVAINGF GRIGRNVVRA LYESGRRAEI TVVAINELAD AAGMAHLLKY DTSHGRFAWE 

        70         80         90        100        110        120 
VRQERDQLFV GDDAIRVLHE RSLQSLPWRE LGVDVVLDCT GVYGSREHGE AHIAAGAKKV 

       130        140        150        160        170        180 
LFSHPGSNDL DATVVYGVNQ DQLRAEHRIV SNASCTTNCI IPVIKLLDDA YGIESGTVTT 

       190        200        210        220        230        240 
IHSAMHDQQV IDAYHPDLRR TRAASQSIIP VDTKLAAGIT RFFPQFNDRF EAIAVRVPTI 

       250        260        270        280        290        300 
NVTAIDLSVT VKKPVKANEV NLLLQKAAQG AFHGIVDYTE LPLVSVDFNH DPHSAIVDGT 

       310        320        330 
QTRVSGAHLI KTLVWCDNEW GFANRMLDTT LAMATVAFR

P0A9B6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools