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UniProtKB/Swiss-Prot entry Q8EIB2

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

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Entry information
Entry name E4PD_SHEON
Primary accession number Q8EIB2
Secondary accession numbers None
Integrated into Swiss-Prot on July 10, 2007
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 46)
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: SO_0931
From
Shewanella oneidensis [TaxID: 70863] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; Shewanellaceae; Shewanella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MR-1;
DOI=10.1038/nbt749; PubMed=12368813 [NCBI, ExPASy, EBI, Israel, Japan]
Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
"Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis.";
Nat. Biotechnol. 20:1118-1123(2002).
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
AE014299; AAN54005.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_716560.1; -.
3D structure databases
HSSP P00362; 1DBV. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q8EIB2.
Enzyme and pathway databases
BioCyc SONE211586:SO_0931-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: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.
Graphical view of domain structure.
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.
Genome annotation databases
GeneID 1168777; -.
GenomeReviews AE014299_GR; SO_0931.
KEGG son:SO_0931; -.
NMPDR fig|211586.1.peg.868; -.
TIGR SO_0931; -.
Phylogenomic databases
HOGENOM Q8EIB2; -.
Other
ProtoNet Q8EIB2.
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_0000293164
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   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: 338 AA [This is the length of the unprocessed precursor] Molecular weight: 37241 Da [This is the MW of the unprocessed precursor] CRC64: FB58AA57643E8006 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIRVAINGYG RIGRSILRAL YESGKRQQIQ IVAINELAKP EAIIHLTQYD TTHGRFQPRV 

        70         80         90        100        110        120 
KLVDGQMQIG DDTIKIFHEP DPAKLPWREL DIDIVYEATG AILDRQSCEA HIHAGAKQVL 

       130        140        150        160        170        180 
ISHPSSADVD GTIVYGVNHD LLRAEHTVVS NASCTTNCIV PVIDVLDKHF GVKSGAITTI 

       190        200        210        220        230        240 
HSAMNDQQVI DAYHDDLRRT RAAGQSIIPV DTKLARGIER ILPHMKDKFE AISVRVPTIN 

       250        260        270        280        290        300 
VTAIDLSVTL DKTVDIATVN QVLELAANGR FNGILGYTDE PLVSCDFNHD PRSSIVDGTQ 

       310        320        330 
TRVSAGQLVK LLLWCDNEWG FANRMLDTSL AMIAAKQS
Q8EIB2 in FASTA format

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