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UniProtKB/Swiss-Prot entry A0L0K7

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

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Entry information
Entry name E4PD_SHESA
Primary accession number A0L0K7
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    November 25, 2008 (Entry version 16)
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: Shewana3_3352
From
Shewanella sp. (strain ANA-3) [TaxID: 94122] [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., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
"Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
Submitted (SEP-2006) 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
CP000469; ABK49576.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_870982.1; -.
3D structure databases
ModBase A0L0K7.
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; 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; 1.
BLOCKS A0L0K7.
ProtoNet A0L0K7.
Genome annotation databases
GeneID 4477653; -.
GenomeReviews CP000469_GR; Shewana3_3352.
KEGG shn:Shewana3_3352; -.
NMPDR fig|94122.5.peg.3360; -.
CMR A0L0K7; Shewana3_3352.
Other
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_0000293165
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: 37233 Da [This is the MW of the unprocessed precursor] CRC64: 9F7D6432154E8C37 [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 
KLVDDQMLIG DDVIKILHEP DPAKLPWREM DIDIVYEATG AILDRNSCEA HILAGAKQVL 

       130        140        150        160        170        180 
ISHPSSADVD GTIVYGVNQD 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 PRSSIIDGTQ 

       310        320        330 
TRVSAGQLVK LLLWCDNEWG FANRMLDTSL AMIAAKQS
A0L0K7 in FASTA format

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