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UniProtKB/Swiss-Prot entry Q87LL0

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

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Entry information
Entry name E4PD_VIBPA
Primary accession number Q87LL0
Secondary accession numbers None
Integrated into Swiss-Prot on July 10, 2007
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 36)
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: VP2601
From
Vibrio parahaemolyticus [TaxID: 670] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RIMD 2210633 / Serotype O3:K6;
DOI=10.1016/S0140-6736(03)12659-1; PubMed=12620739 [NCBI, ExPASy, EBI, Israel, Japan]
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae.";
Lancet 361:743-749(2003).
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
BA000031; BAC60864.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_798980.1; -.
3D structure databases
HSSP P00362; 1GD1. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q87LL0.
Enzyme and pathway databases
BioCyc VPAR223926:VP2601-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: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; FALSE_NEG.
BLOCKS Q87LL0.
Genome annotation databases
GeneID 1190125; -.
GenomeReviews BA000031_GR; VP2601.
KEGG vpa:VP2601; -.
NMPDR fig|223926.1.peg.2601; -.
Phylogenomic databases
HOGENOM Q87LL0; -.
Genome annotation databases
CMR Q87LL0; VP2601.
Other
ProtoNet Q87LL0.
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   345  345     D-erythrose-4-phosphate dehydrogenase. PRO_0000293175
NP_BIND   11    12  2     NAD (By similarity). 
REGION   158   160  3     Substrate binding (Potential). 
REGION   217   218  2     Substrate binding (Potential). 
ACT_SITE   159   159        Nucleophile (By similarity). 
BINDING   204   204        Substrate (Potential). 
BINDING   240   240        Substrate (Potential). 
BINDING   322   322        NAD (By similarity). 
SITE   186   186  1     Activates thiol group during catalysis (By similarity). 
Sequence information
Length: 345 AA [This is the length of the unprocessed precursor] Molecular weight: 38249 Da [This is the MW of the unprocessed precursor] CRC64: 75AA5F1B623DCEE5 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLKVAINGFG RIGRNVLRAV YESGKHQQIK VVAVNELAQP EAMAHLLQYD TSHGRFGKKI 

        70         80         90        100        110        120 
SHDQEHLNVH HESGEYDAIR ILHLSEIELL PWRDLEVDIV LDCTGVYGSK ADGLAHIEAG 

       130        140        150        160        170        180 
AKKVLFSHPG ANDLDNTIIY GVNHETLKDE HRVVSNGSCT TNCIVPIIKV LDEAFGIESG 

       190        200        210        220        230        240 
TITTIHSSMN DQQVIDAYHN DLRRTRAASQ SIIPVDTKLH KGIERIFPKF SNKFEAISVR 

       250        260        270        280        290        300 
VPTVNVTAMD LSVTINTNVK VNDVNQTIVN ASQCTLRNIV DYTESPLVSI DFNHDPHSAI 

       310        320        330        340 
VDGTQTRVSN GQLVKMLVWC DNEWGFANRM LDTALAMKAS SQVEL
Q87LL0 in FASTA format

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