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UniProtKB/Swiss-Prot entry Q1CB62

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

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Entry information
Entry name E4PD_YERPA
Primary accession number Q1CB62
Secondary accession numbers None
Integrated into Swiss-Prot on July 10, 2007
Sequence was last modified on July 11, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 19)
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: YPA_0342
From
Yersinia pestis bv. Antiqua (strain Antiqua) [TaxID: 360102] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Yersinia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.00124-06; PubMed=16740952 [NCBI, ExPASy, EBI, Israel, Japan]
Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen.";
J. Bacteriol. 188:4453-4463(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
CP000308; ABG12310.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_650255.1; -.
3D structure databases
ModBase Q1CB62.
Enzyme and pathway databases
BioCyc YPES360102:YPA_0342-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 Q1CB62.
Genome annotation databases
GeneID 4119735; -.
GenomeReviews CP000308_GR; YPA_0342.
KEGG ypa:YPA_0342; -.
Phylogenomic databases
HOGENOM Q1CB62; -.
Genome annotation databases
CMR Q1CB62; YPA_0342.
Other
ProtoNet Q1CB62.
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   338  338     D-erythrose-4-phosphate dehydrogenase. PRO_0000293179
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: 338 AA [This is the length of the unprocessed precursor] Molecular weight: 37015 Da [This is the MW of the unprocessed precursor] CRC64: 5E0A54DCAD224E06 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAIRIAINGF GRIGRSVLRA LYESGRRAEI SVVAINELAS AEGMAHLLKY DSSHGRFAWD 

        70         80         90        100        110        120 
VRQECDSLYV GDDIIRLIHQ SEIEQLPWSE LGIDVVLDCS GVYGSREDGE AHVASGAKKV 

       130        140        150        160        170        180 
LFAHPGGHDL DATVVYGVNH QDLRAEHRIV SNASCTTNCI IPIIQLLDIA YGIESGTVTT 

       190        200        210        220        230        240 
IHSSMNDQPV IDAYHQDLRR TRAASQSIIP VDTKLAAGIT RIFPKFCDRF EAISVRVPTI 

       250        260        270        280        290        300 
NVTAIDLSVS VTHPVGVAEV NQLLQKAARG AFRGIVDYTE LPLVSMDFNH DPHSAIVDGT 

       310        320        330 
QTRVSGQHLI KTLVWCDNEW GFANRMLDTT LAMAKSGF
Q1CB62 in FASTA format

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