[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY. PubMed=8982014 [NCBI, ExPASy, EBI, Israel, Japan] Carroll P.A., Zhao G., Boyko S.A., Winkler M.E., Calderwood S.B.; "Identification, sequencing, and enzymatic activity of the erythrose-4-phosphate dehydrogenase gene of Vibrio cholerae."; J. Bacteriol. 179:293-296(1997).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Heidelberg J.; Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.

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

U72152; AAC44767.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000627; ABQ20538.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001216003.1; -.

3D structure databases

HSSP

P17721; 1HDG. [HSSP ENTRY / PDB]

ModBase

A5F9G1.

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: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.
Graphical view of domain structure.

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; FALSE_NEG.

Genome annotation databases

GeneID

5136919; -.

GenomeReviews

CP000627_GR; VC0395_A0029.

KEGG

vco:VC0395_A0029; -.

CMR

A5F9G1; VC0395_A0029.

Other

ProtoNet

A5F9G1.

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`
`CHAIN`	`1 341`	`341`	`D-erythrose-4-phosphate dehydrogenase.`	`PRO_0000321845`
`NP_BIND`	`11 12`	`2`	`NAD (By similarity).`
`REGION`	`158 160`	`3`	`Substrate binding (Potential).`
`REGION`	`217 218`	`2`	`Substrate binding (Potential).`
`ACT_SITE`	`159 159`		`Nucleophile (By similarity).`
`BINDING`	`204 204`		`Substrate (Potential).`
`BINDING`	`240 240`		`Substrate (Potential).`
`BINDING`	`322 322`		`NAD (By similarity).`
`SITE`	`186 186`	`1`	`Activates thiol group during catalysis (By similarity).`

Sequence information

Length: 341 AA [This is the length of the unprocessed precursor]

Molecular weight: 37773 Da [This is the MW of the unprocessed precursor]

CRC64: 91DD2A7442C4891D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLRVAINGFG RIGRNVLRAV YESGKRDRIQ VVAVNELAKP DAMAHLLQYD TSHGRFGKKI 

        70         80         90        100        110        120 
SHDQQHIYVH HQNGEYDSIR ILHLSEIPLL PWRDLGVDLV LDCTGVYGCQ EDGQQHIDAG 

       130        140        150        160        170        180 
AKLVLFSHPG ASDLDNTIIY GVNHETLTAE HKIVSNGSCT TNCIVPIIKV LDDAFGIDSG 

       190        200        210        220        230        240 
TITTIHSSMN DQQVIDAYHN DLRRTRAASQ SIIPVDTKLH KGIERIFPKF SNKFEAISVR 

       250        260        270        280        290        300 
VPTVNVTAMD LSVTIKSNVK VNDVNQTIVN ASQCTLRGIV DYTEAPLVSI DFNHDPHSAI 

       310        320        330        340 
VDGTQTRVSN GQLVKMLVWC DNEWGFANRM LDTALAMQAT Q

A5F9G1 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