ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q3YXU5

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name E4PD_SHISS
Primary accession number Q3YXU5
Secondary accession numbers None
Integrated into Swiss-Prot on July 10, 2007
Sequence was last modified on September 27, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 26)
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: SSON_3079
From
Shigella sonnei (strain Ss046) [TaxID: 300269] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Shigella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gki954; PubMed=16275786 [NCBI, ExPASy, EBI, Israel, Japan]
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.;
"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery.";
Nucleic Acids Res. 33:6445-6458(2005).
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
CP000038; AAZ89667.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_311902.1; -.
3D structure databases
ModBase Q3YXU5.
Enzyme and pathway databases
BioCyc SSON300269:SSO_3079-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 Q3YXU5.
Genome annotation databases
GeneID 3669214; -.
GenomeReviews CP000038_GR; SSON_3079.
KEGG ssn:SSON_3079; -.
Phylogenomic databases
HOGENOM Q3YXU5; -.
Genome annotation databases
CMR Q3YXU5; SSON_3079.
Other
ProtoNet Q3YXU5.
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_0000293172
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
Q3YXU5 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!