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UniProtKB/Swiss-Prot entry Q10208


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

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Entry information
Entry name KPYK_SCHPO
Primary accession number Q10208
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 64)
Name and origin of the protein
Protein name Pyruvate kinase
Synonyms PK
EC 2.7.1.40
Gene name
Name: pyk1
ORFNames: SPAC4H3.10c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0378-1097(95)00408-3; PubMed=8586271 [NCBI, ExPASy, EBI, Israel, Japan]
Nairn J., Smith S., Allison P.J., Rigden D., Fothergill-Gilmore L.A., Price N.C.;
"Cloning and sequencing of a gene encoding pyruvate kinase from Schizosaccharomyces pombe; implications for quaternary structure and regulation of the enzyme.";
FEMS Microbiol. Lett. 134:221-226(1995).
[2]
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).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-63; SER-281 AND SER-412, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
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
X91008; CAA62490.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329670; CAA93349.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T38890; T38890.
T45166; T45166.
RefSeq NP_594346.1; -.
3D structure databases
HSSP P00549; 1A3W. [HSSP ENTRY / PDB]
ModBase Q10208.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-002453-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC4H3.10c; -.
Gene expression databases
ArrayExpress Q10208; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from InterPro).
GO:0030955; Molecular function: potassium ion binding (inferred from electronic annotation from InterPro).
GO:0004743; Molecular function: pyruvate kinase activity (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001697; Pyr_Knase.
IPR015813; Pyrv/PenolPyrv_Kinase_cat.
IPR015794; Pyrv_Knase_a/b.
IPR015793; Pyrv_Knase_brl.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
G3DSA:3.40.1380.20; Pyrv_Knase_a/b; 1.
PANTHER PTHR11817; Pyruvate_kinase; 1.
Pfam PF00224; PK; 1.
PF02887; PK_C; 1.
Pfam graphical view of domain structure.
PRINTS PR01050; PYRUVTKNASE.
ProDom PD001009; Pyruvate_kinase; 2.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01064; pyruv_kin; 1.
PROSITE PS00110; PYRUVATE_KINASE; 1.
ProtoNet Q10208.
Genome annotation databases
GeneID 2543557; -.
KEGG spo:SPAC4H3.10c; -.
NMPDR fig|4896.1.peg.4316; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Kinase; Magnesium; Metal-binding; Phosphoprotein; Pyruvate; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   509  509     Pyruvate kinase. PRO_0000112118
ACT_SITE   247   247        By similarity. 
METAL   249   249        Magnesium (Potential). 
METAL   270   270        Magnesium (Potential). 
METAL   271   271        Magnesium (Potential). 
BINDING   344   344        ADP (Potential). 
MOD_RES   29    29        Phosphoserine. 
MOD_RES   63    63        Phosphoserine. 
MOD_RES   281   281        Phosphoserine. 
MOD_RES   412   412        Phosphoserine. 
CONFLICT   391   391        A -> R (in Ref. 1; CAA62490). 
Sequence information
Length: 509 AA [This is the length of the unprocessed precursor] Molecular weight: 55515 Da [This is the MW of the unprocessed precursor] CRC64: 589378533FCFD5F7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSSAVSPKQ WVAGLNSELD IPAVNRRTSI ICTIGPKSNN VETLCKLRDA GMNIVRMNFS 

        70         80         90        100        110        120 
HGSYEYHQSV IDNARKASAT NPLFPLAIAL DTKGPEIRTG LTVGGTDYPI SSGHEMIFTT 

       130        140        150        160        170        180 
DDAYAEKCND KVMYIDYKNI TKVIQPGRII YVDDGILSFT VIEKVDDKNL KVRVNNNGKI 

       190        200        210        220        230        240 
SSKKGVNLPK TDVDLPALSE KDKADLRFGV KNGVDMIFAS FIRRAEDVIH IREVLGEEGK 

       250        260        270        280        290        300 
NIKIICKIEN QQGVNNFDSI LDVTDGIMVA RGDLGIEIPA SQVFVAQKMM IAKCNIAGKP 

       310        320        330        340        350        360 
VACATQMLES MTYNPRPTRA EVSDVGNAVL DGADLVMLSG ETTKGSYPVE AVTYMAETAR 

       370        380        390        400        410        420 
VAEASIPYGS LYQEMFGLVR RPLECATETT AVAAIGASIE SDAKAIVVLS TSGNTARLCS 

       430        440        450        460        470        480 
KYRPSIPIVM VTRCPQRARQ SHLNRGVYPV IYEKEPLSDW QKDVDARVAY GCQQAYKMNI 

       490        500 
LKKGDKIIVL QGAVGGKGHT SIFRLTVAE 

Q10208 in FASTA format

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