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UniProtKB/Swiss-Prot entry A0KGD2

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

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Entry information
Entry name E4PD_AERHH
Primary accession number A0KGD2
Secondary accession numbers None
Integrated into Swiss-Prot on July 10, 2007
Sequence was last modified on December 12, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 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: AHA_0780
From
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [TaxID: 380703] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; Aeromonadaceae; Aeromonas.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.00621-06; PubMed=16980456 [NCBI, ExPASy, EBI, Israel, Japan]
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
J. Bacteriol. 188:8272-8282(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
CP000462; ABK36491.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_855322.1; -.
3D structure databases
ModBase A0KGD2.
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; FALSE_NEG.
BLOCKS A0KGD2.
Genome annotation databases
GeneID 4487940; -.
GenomeReviews CP000462_GR; AHA_0780.
KEGG aha:AHA_0780; -.
TIGR AHA_0780; -.
Other
ProtoNet A0KGD2.
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   336  336     D-erythrose-4-phosphate dehydrogenase. PRO_0000293143
NP_BIND   11    12  2     NAD (By similarity). 
REGION   153   155  3     Substrate binding (Potential). 
REGION   212   213  2     Substrate binding (Potential). 
ACT_SITE   154   154        Nucleophile (By similarity). 
BINDING   80    80        NAD; via carbonyl oxygen (By similarity). 
BINDING   199   199        Substrate (Potential). 
BINDING   235   235        Substrate (Potential). 
BINDING   317   317        NAD (By similarity). 
SITE   181   181  1     Activates thiol group during catalysis (By similarity). 
Sequence information
Length: 336 AA [This is the length of the unprocessed precursor] Molecular weight: 36832 Da [This is the MW of the unprocessed precursor] CRC64: D799CCDE4474D1ED [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIKIAINGYG RIGRNVLRAL YESGRDKNIK IVAINELAAP EAMVHLTRFD TSHGRFHHPV 

        70         80         90        100        110        120 
QLAGNSMLVG EDLISLFAER DPSRLPWRAL GVDVVLDCTG VFGSRADAEL HLAAGAGKVL 

       130        140        150        160        170        180 
FSHPAEADVD ATIVYGVNHQ VLTGRERIVS NASCTTNCVV PVIETLHREF EINCGTITTI 

       190        200        210        220        230        240 
HSAMHDQQVI DAYHSDLRRT RAASQSIIPV DTKLAKGLER ILPHFAGKFE AIAVRVPTIN 

       250        260        270        280        290        300 
VTAMDLSITV RKKVTVTDVN QALQRASRGT LSGILDYTEE PLVSVDFNHD AHSCIIDGTQ 

       310        320        330 
TRVSDANLVK MLMWCDNEWG FANRMLDTTR AMMAAG
A0KGD2 in FASTA format

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