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UniProtKB/Swiss-Prot entry Q9P6Q2


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

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Entry information
Entry name ENOPH_SCHPO
Primary accession number Q9P6Q2
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 38)
Name and origin of the protein
Protein name Enolase-phosphatase E1
Synonyms EC 3.1.3.77
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Gene name
ORFNames: SPAC644.08
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(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
CU329670; CAB90135.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_593876.1; -.
3D structure databases
ModBase Q9P6Q2.
Organism-specific databases
GeneDB_Spombe SPAC644.08; -.
Gene expression databases
ArrayExpress Q9P6Q2; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0043874; Molecular function: acireductone synthase activity (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008967; Molecular function: phosphoglycolate phosphatase activity (inferred from electronic annotation from InterPro).
GO:0009086; Biological process: methionine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0019509; Biological process: methionine salvage (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR005834; Dehalogen-like_hydro.
IPR010041; Enolase_ppase.
IPR006439; HAD-SF_hydro_IA_v1.
Graphical view of domain structure.
PANTHER PTHR20371; Enolase_ppase; 1.
Pfam PF00702; Hydrolase; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01691; enolase-ppase; 1.
TIGR01549; HAD-SF-IA-v1; 1.
ProtoNet Q9P6Q2.
Genome annotation databases
GeneID 2543661; -.
KEGG spo:SPAC644.08; -.
NMPDR fig|4896.1.peg.3846; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding; Methionine biosynthesis; Nucleus.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   216  216     Enolase-phosphatase E1. PRO_0000314113
REGION   115   116  2     Substrate binding (By similarity). 
METAL   8     8        Magnesium (By similarity). 
METAL   10    10        Magnesium; via carbonyl oxygen (By similarity). 
METAL   172   172        Magnesium (By similarity). 
BINDING   149   149        Substrate (By similarity). 
Sequence information
Length: 216 AA [This is the length of the unprocessed precursor] Molecular weight: 24424 Da [This is the MW of the unprocessed precursor] CRC64: D5FE2EE20F619F59 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVKNLLLDIE GTVGSISFVK DKLFPYAASR YESYVNENYE SDENLRELGK TPEEALINLR 

        70         80         90        100        110        120 
KLHAEGSKER SFKMVQGRIW KKGYESNELT SHLFPDVVPA IQRSLQLGMR VYIYSSGSVP 

       130        140        150        160        170        180 
AQKLYFEHSD AGNLLKYFSG YYDTTIGLKT ECGSYVKIVG NSNPREWLFL SDNINELKAA 

       190        200        210 
RKVGLHTGLV VRPGNDPVVD TSGFPVYNSF EILFTE 

Q9P6Q2 in FASTA format

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