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UniProtKB/Swiss-Prot entry P0C6C2

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name E4PD_VIBCH
Primary accession number P0C6C2
Secondary accession numbers P96153 Q9KUN9
Integrated into Swiss-Prot on February 26, 2008
Sequence was last modified on February 26, 2008 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 9)
Name and origin of the protein
Protein name D-erythrose-4-phosphate dehydrogenase
Synonyms E4PDH
EC 1.2.1.72
Gene name
Name: epd
OrderedLocusNames: VC_0476
From
Vibrio cholerae [TaxID: 666] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 39315 / El Tor Inaba N16961 / Serotype O1;
DOI=10.1038/35020000; PubMed=10952301 [NCBI, ExPASy, EBI, Israel, Japan]
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae.";
Nature 406:477-483(2000).
Comments
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
AE003852; AAF93649.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E82317; E82317.
RefSeq NP_230130.2; -.
3D structure databases
HSSP P17721; 1HDG. [HSSP ENTRY / PDB]
ModBase P0C6C2.
Ontologies
GO
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 2615270; -.
GenomeReviews AE003852_GR; VC_0476.
KEGG vch:VC0476; -.
TIGR VC_0476; -.
Other
ProtoNet P0C6C2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   341  341     D-erythrose-4-phosphate dehydrogenase. PRO_0000293173
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
P0C6C2 in FASTA format

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