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UniProtKB/Swiss-Prot entry Q7CPU5

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

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Entry information
Entry name E4PD_SALTY
Primary accession number Q7CPU5
Secondary accession numbers None
Integrated into Swiss-Prot on July 10, 2007
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 32)
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: STM3070
From
Salmonella typhimurium [TaxID: 602] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan]
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
Nature 413:852-856(2001).
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
AE008841; AAL21945.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_461986.1; -.
3D structure databases
HSSP P06977; 1DC5. [HSSP ENTRY / PDB]
ModBase Q7CPU5.
Enzyme and pathway databases
BioCyc STYP99287:STM3070-MON; -.
Organism-specific databases
StyGene SG?????; epd.
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.
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.
ProtoNet Q7CPU5.
Genome annotation databases
GeneID 1254593; -.
GenomeReviews AE006468_GR; STM3070.
KEGG stm:STM3070; -.
Phylogenomic databases
HOGENOM Q7CPU5; -.
Genome annotation databases
CMR Q7CPU5; STM3070.
Other
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   348  348     D-erythrose-4-phosphate dehydrogenase. PRO_0000293159
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: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 38125 Da [This is the MW of the unprocessed precursor] CRC64: 5009E1EFBB31413A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTVRIAINGF GRIGRNVVRA LYESGRRAEI TVVAINELAD AAGMAHLLKY DTSHGRFAWE 

        70         80         90        100        110        120 
VRHEREQLFV GDDVIRILHE RTLADLPWRE LGVDVVLDCT GVYGNREHGE AHIAAGAKKV 

       130        140        150        160        170        180 
LFSHPGSNDL DATVVFGVNQ NQLRAEHRIV SNASCTTNCI IPVIKLLDDA YGIESGTVTT 

       190        200        210        220        230        240 
IHSAMNDQQV IDAYHSDLRR TRAASQSIIP VDTKLAAGIT RIFPQFNDRF EAIAVRVPTI 

       250        260        270        280        290        300 
NVTAIDLSVT VKKPVKASEV NQLLQKAAQG AFHGIVDYTE SPLVSIDFNH DPHSAIVDGT 

       310        320        330        340 
QTRVSGAHLI KTLVWCDNEW GFANRMLDTT LAMAAVGFRL DASASTKL
Q7CPU5 in FASTA format

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