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UniProtKB/Swiss-Prot entry Q0TDS9

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

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Entry information
Entry name E4PD_ECOL5
Primary accession number Q0TDS9
Secondary accession numbers None
Integrated into Swiss-Prot on July 10, 2007
Sequence was last modified on September 5, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 18)
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: ECP_2916
From
Escherichia coli O6:K15:H31 (strain 536 / UPEC) [TaxID: 362663] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1111/j.1365-2958.2006.05255.x; PubMed=16879640 [NCBI, ExPASy, EBI, Israel, Japan]
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536.";
Mol. Microbiol. 61:584-595(2006).
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
CP000247; ABG70900.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_670801.1; -.
3D structure databases
ModBase Q0TDS9.
Enzyme and pathway databases
BioCyc ECOL362663:ECP_2916-MON; -.
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; 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 Q0TDS9.
Genome annotation databases
GeneID 4190960; -.
GenomeReviews CP000247_GR; ECP_2916.
KEGG ecp:ECP_2916; -.
Phylogenomic databases
HOGENOM Q0TDS9; -.
Genome annotation databases
CMR Q0TDS9; ECP_2916.
Other
ProtoNet Q0TDS9.
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
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   339  338     D-erythrose-4-phosphate dehydrogenase. PRO_0000293147
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: 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
Q0TDS9 in FASTA format

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