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UniProtKB/Swiss-Prot entry A4WE72

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

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Entry information
Entry name E4PD_ENT38
Primary accession number A4WE72
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on May 29, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 14)
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: Ent638_3340
From
Enterobacter sp. (strain 638) [TaxID: 399742] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Enterobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
"Complete sequence of chromosome of Enterobacter sp. 638.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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
CP000653; ABP62002.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001178053.1; -.
3D structure databases
ModBase A4WE72.
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: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; 2.
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 A4WE72.
Genome annotation databases
GeneID 5111854; -.
GenomeReviews CP000653_GR; Ent638_3340.
KEGG ent:Ent638_3340; -.
NMPDR fig|399742.4.peg.3181; -.
CMR A4WE72; Ent638_3340.
Other
ProtoNet A4WE72.
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   339  339     D-erythrose-4-phosphate dehydrogenase. PRO_1000069894
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   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: 37248 Da [This is the MW of the unprocessed precursor] CRC64: F1E4C31BEFFF7A1B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTVRVAINGF GRIGRNVIRA LYESGRRAEI TVVAINELAD AVGMAHLLKY DTSHGRFAWD 

        70         80         90        100        110        120 
VRQEREQLFV GDDAIRVLHE QSIDALPWRE LGVDVVLDCT GVYGNREHGE AHLAAGAKKV 

       130        140        150        160        170        180 
LFSHPGGHDL DATVVYGVNH HELQAEHRIV SNASCTTNCI IPVIKLLDDA YGIESGTVTT 

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

       250        260        270        280        290        300 
NVTAIDLSVT VKKPVKASEV NLLLQKAAQG SFHGIVDYTE LPLVSVDFNH DPHSAIVDGT 

       310        320        330 
QTRVSGAHLI KTLVWCDNEW GFANRMLDTT LAMAAQGFR
A4WE72 in FASTA format

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