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UniProtKB/Swiss-Prot entry B0TUC0

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

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Entry information
Entry name E4PD_SHEHH
Primary accession number B0TUC0
Secondary accession numbers None
Integrated into Swiss-Prot on May 20, 2008
Sequence was last modified on April 8, 2008 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 8)
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: Shal_0845
From
Shewanella halifaxensis (strain HAW-EB4) [TaxID: 458817] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; Shewanellaceae; Shewanella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
"Complete sequence of Shewanella halifaxensis HAW-EB4.";
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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
CP000931; ABZ75420.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001673079.1; -.
3D structure databases
ModBase B0TUC0.
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.
PROSITE PS00071; GAPDH; 1.
Genome annotation databases
GeneID 5902965; -.
GenomeReviews CP000931_GR; Shal_0845.
KEGG shl:Shal_0845; -.
CMR B0TUC0; Shal_0845.
Other
ProtoNet B0TUC0.
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   339  339     D-erythrose-4-phosphate dehydrogenase. PRO_1000088209
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: 339 AA [This is the length of the unprocessed precursor] Molecular weight: 37808 Da [This is the MW of the unprocessed precursor] CRC64: 2C0081DF3286173C [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIRVAINGYG RIGRSILRAL YESAKRDRIQ IVAINELAKP EAMLHLTQYD TTHGRFHTQV 

        70         80         90        100        110        120 
KLDNQHMIIG DDAIKLLHEP NPANLPWKEL DIDIVYEATG VINDRQECEA HLKAGAKQVL 

       130        140        150        160        170        180 
ISHPSSNDVD ATIVYGVNQD LLRAEHTVVS NASCTTNCIV PVIDVLDRHF EVKSGAITTI 

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

       250        260        270        280        290        300 
VTAIDLSVTL NKRVDIELVN RVLKQATEGS FSGVVGFTNE PLVSCDFNHD PRSSIVDGTQ 

       310        320        330 
TRVSDGHLVK LLLWCDNEWG FANRMLDTSL EMIKAKRSS
B0TUC0 in FASTA format

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