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UniProtKB/Swiss-Prot entry Q12QA4

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

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Entry information
Entry name E4PD_SHEDO
Primary accession number Q12QA4
Secondary accession numbers None
Integrated into Swiss-Prot on July 10, 2007
Sequence was last modified on July 10, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 22)
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: Sden_1084
From
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) [TaxID: 318161] [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., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of Shewanella denitrificans OS217.";
Submitted (MAR-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
CP000302; ABE54372.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_562095.1; -.
3D structure databases
ModBase Q12QA4.
Enzyme and pathway databases
BioCyc SDEN318161:SDEN_1084-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 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.
PROSITE PS00071; GAPDH; 1.
Genome annotation databases
GeneID 4017367; -.
GenomeReviews CP000302_GR; Sden_1084.
KEGG sdn:Sden_1084; -.
NMPDR fig|318161.14.peg.1066; -.
Phylogenomic databases
HOGENOM Q12QA4; -.
Genome annotation databases
CMR Q12QA4; Sden_1084.
Other
ProtoNet Q12QA4.
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   342  342     D-erythrose-4-phosphate dehydrogenase. PRO_0000293161
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: 342 AA [This is the length of the unprocessed precursor] Molecular weight: 37587 Da [This is the MW of the unprocessed precursor] CRC64: CB10920796C0C700 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIRVAINGYG RIGRSILRAL YESGKRQQIQ IVAINELAKP EAIRHLTQYD TTHGRFGQTV 

        70         80         90        100        110        120 
ELQEGKLHIG DDAIALFHQS DATKLPWGEL DIDIVFEASG SLIEREACEA HIISGAKQVL 

       130        140        150        160        170        180 
ISHPSSQDVD ATIVYGVNHH LLAAEHTVVS NASCTTNCIV PVIDVLDSHF GVISGAITTI 

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

       250        260        270        280        290        300 
VTAIDVSVTL RDRVDISIIN SVLQQAAKGR FDGILGYTDE PLVSCDFNHD PRSSIVDATQ 

       310        320        330        340 
TRVSDGHLVK LLLWCDNEWG FANRMLDTSL AMIRAKSAKS VK
Q12QA4 in FASTA format

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