NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.01726-06; PubMed=17293413 [NCBI, ExPASy, EBI, Israel, Japan]
Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
"The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes.";
J. Bacteriol. 189:3228-3236(2007).

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.
PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 1/5 .
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. Epd subfamily.

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

CP000468; ABJ02351.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_854140.1; -.

3D structure databases

ModBase

A1AFB1.

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: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.

BLOCKS

A1AFB1.

Genome annotation databases

GeneID

4495158; -.

GenomeReviews

CP000468_GR; Ecok1_28570.

KEGG

ecv:APECO1_3606; -.

CMR

A1AFB1; Ecok1_28570.

Other

ProtoNet

A1AFB1.

UniRef

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

Keywords

Complete proteome; Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 339`	`338`	`D-erythrose-4-phosphate dehydrogenase.`	`PRO_0000293146`
`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).`

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: BE77BF793D9F09BD [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 DTTVVYGVNQ 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 AFHGIVDYAE LPLVSVDFNH DPHSAIVDGT 

       310        320        330 
QTRVSGAHLI KTLVWCDNEW GFANRMLDTT LAMATVAFR

A1AFB1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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