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UniProtKB/Swiss-Prot entry P00549


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

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Entry information
Entry name KPYK1_YEAST
Primary accession number P00549
Secondary accession number Q2VQG5
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 1, 1989 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 99)
Name and origin of the protein
Protein name Pyruvate kinase 1
Synonyms PK 1
EC 2.7.1.40
Gene name
Name: PYK1
Synonyms: CDC19
OrderedLocusNames: YAL038W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0014-5793(89)81359-6; PubMed=2653861 [NCBI, ExPASy, EBI, Israel, Japan]
McNally T., Purvis I.J., Fothergill-Gilmore L.A., Brown A.L.P.;
"The yeast pyruvate kinase gene does not contain a string of non-preferred codons: revised nucleotide sequence.";
FEBS Lett. 247:312-316(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6185493 [NCBI, ExPASy, EBI, Israel, Japan]
Burke R.L., Tekamp-Olson P., Najarian R.;
"The isolation, characterization, and sequence of the pyruvate kinase gene of Saccharomyces cerevisiae.";
J. Biol. Chem. 258:2193-2201(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 76625 / YPH499, Ba194, Bb32, Fy93, M1-2A, M2-8, M5-7A, M5-7B, M7-8D, MMR2-1, MMR2-3, MMR2-5, MMW1-12, MMW1-15, MMW1-15h2, MMW1-2, MMW1-2h2, ORM1-1, Sgu52E, Sgu52F, YPS396, YPS400, YPS598, YPS600, YPS602, YPS604, YPS606, YPS608, and YPS610;
DOI=10.1111/j.1567-1364.2006.00059.x; PubMed=16879422 [NCBI, ExPASy, EBI, Israel, Japan]
Aa E., Townsend J.P., Adams R.I., Nielsen K.M., Taylor J.W.;
"Population structure and gene evolution in Saccharomyces cerevisiae.";
FEMS Yeast Res. 6:702-715(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=7731988 [NCBI, ExPASy, EBI, Israel, Japan]
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.;
"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-22; THR-372; SER-402; THR-478 AND SER-498, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-22 AND THR-478, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-9; SER-53; SER-56 AND SER-213, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; THR-21 AND SER-22, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-9; SER-16; SER-22; THR-26; SER-53; SER-332; SER-402; THR-403; THR-407; SER-450; THR-478 AND TYR-479, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[12]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
DOI=10.1016/S0969-2126(98)00021-5; PubMed=9519410 [NCBI, ExPASy, EBI, Israel, Japan]
Jurica M.S., Mesecar A., Heath P.J., Shi W., Nowak T., Stoddard B.L.;
"The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate.";
Structure 6:195-210(1998).
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
V01321; CAA24631.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14400; CAA32573.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949862; AAY27264.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949863; AAY27265.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949864; AAY27266.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949865; AAY27267.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949866; AAY27268.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949867; AAY27269.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949868; AAY27270.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949869; AAY27271.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949870; AAY27272.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949871; AAY27273.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949872; AAY27274.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949873; AAY27275.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949874; AAY27276.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949875; AAY27277.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949876; AAY27278.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949877; AAY27279.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949878; AAY27280.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949879; AAY27281.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949880; AAY27282.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949881; AAY27283.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949882; AAY27284.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949883; AAY27285.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949884; AAY27286.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949885; AAY27287.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949886; AAY27288.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949887; AAY27289.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949888; AAY27290.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949889; AAY27291.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY949890; AAY27292.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12980; AAC04993.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY693107; AAT93126.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S05764; KIBYP.
RefSeq NP_009362.1; -.
3D structure databases
PDB
1A3W; X-ray; 3.00 A; A/B=1-500.[ExPASy / RCSB / EBI]
1A3X; X-ray; 3.00 A; A/B=1-500.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A3W; -.
1A3X; -.
ModBase P00549.
Protein-protein interaction databases
DIP DIP:4124N; -.
IntAct P00549; -.
2D gel databases
COMPLUYEAST-2DPAGE P00549; -.
Organism-specific databases
CYGD YAL038w; -.
SGD S000000036; CDC19.
Yeast-GFP YAL038W.
Gene expression databases
ArrayExpress P00549; -.
GermOnline YAL038W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0004743; Molecular function: pyruvate kinase activity (inferred from direct assay from SGD).
GO:0006096; Biological process: glycolysis (inferred from mutant phenotype from SGD).
GO:0006090; Biological process: pyruvate metabolic process (inferred from mutant phenotype from SGD).
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.
BLOCKS P00549.
ProtoNet P00549.
Proteomic databases
PeptideAtlas P00549; -.
Genome annotation databases
Ensembl YAL038W; Saccharomyces cerevisiae. [Contig view]
GeneID 851193; -.
GenomeReviews U00091_GR; YAL038W.
KEGG sce:YAL038W; -.
NMPDR fig|4932.3.peg.39; -.
Phylogenomic databases
HOGENOM P00549; -.
Other
LinkHub P00549; -.
NextBio 968037; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Allosteric enzyme; Complete proteome; Glycolysis; Kinase; Magnesium; Metal-binding; Phosphoprotein; Pyruvate; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   500  500     Pyruvate kinase 1. PRO_0000112121
ACT_SITE   240   240        By similarity. 
METAL   242   242        Magnesium (Potential). 
METAL   263   263        Magnesium (Potential). 
METAL   264   264        Magnesium (Potential). 
BINDING   337   337        ADP (Potential). 
MOD_RES   8     8        Phosphothreonine. 
MOD_RES   9     9        Phosphoserine. 
MOD_RES   16    16        Phosphoserine. 
MOD_RES   21    21        Phosphothreonine. 
MOD_RES   22    22        Phosphoserine. 
MOD_RES   26    26        Phosphothreonine. 
MOD_RES   53    53        Phosphoserine. 
MOD_RES   56    56        Phosphoserine. 
MOD_RES   213   213        Phosphoserine. 
MOD_RES   332   332        Phosphoserine. 
MOD_RES   372   372        Phosphothreonine. 
MOD_RES   402   402        Phosphoserine. 
MOD_RES   403   403        Phosphothreonine. 
MOD_RES   407   407        Phosphothreonine. 
MOD_RES   450   450        Phosphoserine. 
MOD_RES   478   478        Phosphothreonine. 
MOD_RES   479   479        Phosphotyrosine. 
MOD_RES   498   498        Phosphoserine. 
CONFLICT   382   386        VAASA -> SLPR (in Ref. 1; CAA24631). 
HELIX   3     8  6      
HELIX   29    31  3      
HELIX   34    43  10      
STRAND   47    49  3      
HELIX   57    73  17      
STRAND   82    84  3      
STRAND   96    99  4      
STRAND   108   112  5      
TURN   116   120  5      
STRAND   126   129  4      
HELIX   133   136  4      
STRAND   142   145  4      
TURN   146   149  4      
STRAND   150   153  4      
STRAND   163   167  5      
STRAND   178   180  3      
HELIX   193   205  13      
STRAND   208   212  5      
HELIX   218   232  15      
STRAND   235   241  7      
HELIX   245   248  4      
HELIX   250   256  7      
STRAND   260   262  3      
HELIX   264   270  7      
HELIX   273   275  3      
HELIX   276   290  15      
STRAND   294   296  3      
HELIX   302   305  4      
HELIX   312   324  13      
STRAND   327   329  3      
TURN   333   337  5      
HELIX   341   355  15      
HELIX   361   368  8      
HELIX   378   393  16      
STRAND   398   401  4      
STRAND   403   405  3      
HELIX   406   413  8      
STRAND   420   425  6      
HELIX   429   432  4      
HELIX   433   435  3      
STRAND   439   443  5      
TURN   452   454  3      
HELIX   455   469  15      
STRAND   478   483  6      
TURN   487   489  3      
STRAND   494   499  6      
Sequence information
Length: 500 AA [This is the length of the unprocessed precursor] Molecular weight: 54545 Da [This is the MW of the unprocessed precursor] CRC64: 78D753FC410C5820 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSRLERLTSL NVVAGSDLRR TSIIGTIGPK TNNPETLVAL RKAGLNIVRM NFSHGSYEYH 

        70         80         90        100        110        120 
KSVIDNARKS EELYPGRPLA IALDTKGPEI RTGTTTNDVD YPIPPNHEMI FTTDDKYAKA 

       130        140        150        160        170        180 
CDDKIMYVDY KNITKVISAG RIIYVDDGVL SFQVLEVVDD KTLKVKALNA GKICSHKGVN 

       190        200        210        220        230        240 
LPGTDVDLPA LSEKDKEDLR FGVKNGVHMV FASFIRTAND VLTIREVLGE QGKDVKIIVK 

       250        260        270        280        290        300 
IENQQGVNNF DEILKVTDGV MVARGDLGIE IPAPEVLAVQ KKLIAKSNLA GKPVICATQM 

       310        320        330        340        350        360 
LESMTYNPRP TRAEVSDVGN AILDGADCVM LSGETAKGNY PINAVTTMAE TAVIAEQAIA 

       370        380        390        400        410        420 
YLPNYDDMRN CTPKPTSTTE TVAASAVAAV FEQKAKAIIV LSTSGTTPRL VSKYRPNCPI 

       430        440        450        460        470        480 
ILVTRCPRAA RFSHLYRGVF PFVFEKEPVS DWTDDVEARI NFGIEKAKEF GILKKGDTYV 

       490        500 
SIQGFKAGAG HSNTLQVSTV 

P00549 in FASTA format

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View entry in raw text format (no links)
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