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P00549 (KPYK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate kinase 1

Short name=PK 1
EC=2.7.1.40
Alternative name(s):
cell division cycle protein 19
Gene names
Name:CDC19
Synonyms:PYK1
Ordered Locus Names:YAL038W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium.

Potassium.

Enzyme regulation

The activity is regulated by glucose levels. Activated by fructose-1,6-bisphosphate.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.

Subunit structure

Homotetramer.

Miscellaneous

Present with 291000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the pyruvate kinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 500499Pyruvate kinase 1
PRO_0000112121

Sites

Metal binding511Potassium By similarity
Metal binding531Potassium By similarity
Metal binding841Potassium By similarity
Metal binding851Potassium; via carbonyl oxygen By similarity
Metal binding2421Magnesium Potential
Metal binding2661Magnesium By similarity
Binding site491Substrate By similarity
Binding site2651Substrate; via amide nitrogen By similarity
Binding site2661Substrate; via amide nitrogen By similarity
Binding site2981Substrate By similarity
Binding site3371ADP Potential
Site2401Transition state stabilizer By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.10
Modified residue91Phosphoserine Ref.9 Ref.12
Modified residue161Phosphoserine Ref.11 Ref.12
Modified residue311Phosphothreonine Ref.12
Modified residue701Phosphoserine Ref.12
Modified residue1841Phosphothreonine Ref.12
Modified residue2131Phosphoserine Ref.10
Modified residue3161Phosphoserine Ref.12
Modified residue4501Phosphoserine Ref.12
Modified residue4781Phosphothreonine Ref.9 Ref.12

Experimental info

Sequence conflict382 – 3865VAASA → SLPR in CAA24631. Ref.1

Secondary structure

............................................................................................. 500
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00549 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 78D753FC410C5820

FASTA50054,545
        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 

« Hide

References

« Hide 'large scale' references
[1]"The yeast pyruvate kinase gene does not contain a string of non-preferred codons: revised nucleotide sequence."
McNally T., Purvis I.J., Fothergill-Gilmore L.A., Brown A.L.P.
FEBS Lett. 247:312-316(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The isolation, characterization, and sequence of the pyruvate kinase gene of Saccharomyces cerevisiae."
Burke R.L., Tekamp-Olson P., Najarian R.
J. Biol. Chem. 258:2193-2201(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Population structure and gene evolution in Saccharomyces cerevisiae."
Aa E., Townsend J.P., Adams R.I., Nielsen K.M., Taylor J.W.
FEMS Yeast Res. 6:702-715(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.
[4]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
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.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND THR-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
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.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-16; THR-31; SER-70; THR-184; SER-316; SER-450 AND THR-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate."
Jurica M.S., Mesecar A., Heath P.J., Shi W., Nowak T., Stoddard B.L.
Structure 6:195-210(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01321 Genomic DNA. Translation: CAA24631.1.
X14400 Genomic DNA. Translation: CAA32573.1.
AY949862 Genomic DNA. Translation: AAY27264.1.
AY949863 Genomic DNA. Translation: AAY27265.1.
AY949864 Genomic DNA. Translation: AAY27266.1.
AY949865 Genomic DNA. Translation: AAY27267.1.
AY949866 Genomic DNA. Translation: AAY27268.1.
AY949867 Genomic DNA. Translation: AAY27269.1.
AY949868 Genomic DNA. Translation: AAY27270.1.
AY949869 Genomic DNA. Translation: AAY27271.1.
AY949870 Genomic DNA. Translation: AAY27272.1.
AY949871 Genomic DNA. Translation: AAY27273.1.
AY949872 Genomic DNA. Translation: AAY27274.1.
AY949873 Genomic DNA. Translation: AAY27275.1.
AY949874 Genomic DNA. Translation: AAY27276.1.
AY949875 Genomic DNA. Translation: AAY27277.1.
AY949876 Genomic DNA. Translation: AAY27278.1.
AY949877 Genomic DNA. Translation: AAY27279.1.
AY949878 Genomic DNA. Translation: AAY27280.1.
AY949879 Genomic DNA. Translation: AAY27281.1.
AY949880 Genomic DNA. Translation: AAY27282.1.
AY949881 Genomic DNA. Translation: AAY27283.1.
AY949882 Genomic DNA. Translation: AAY27284.1.
AY949883 Genomic DNA. Translation: AAY27285.1.
AY949884 Genomic DNA. Translation: AAY27286.1.
AY949885 Genomic DNA. Translation: AAY27287.1.
AY949886 Genomic DNA. Translation: AAY27288.1.
AY949887 Genomic DNA. Translation: AAY27289.1.
AY949888 Genomic DNA. Translation: AAY27290.1.
AY949889 Genomic DNA. Translation: AAY27291.1.
AY949890 Genomic DNA. Translation: AAY27292.1.
U12980 Genomic DNA. Translation: AAC04993.1.
AY693107 Genomic DNA. Translation: AAT93126.1.
BK006935 Genomic DNA. Translation: DAA06948.1.
PIRKIBYP. S05764.
RefSeqNP_009362.1. NM_001178183.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3WX-ray3.00A/B1-500[»]
1A3XX-ray3.00A/B1-500[»]
ProteinModelPortalP00549.
SMRP00549. Positions 2-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31727. 144 interactions.
DIPDIP-4124N.
IntActP00549. 182 interactions.
MINTMINT-565419.
STRING4932.YAL038W.

2D gel databases

COMPLUYEAST-2DPAGEP00549.

Proteomic databases

PaxDbP00549.
PeptideAtlasP00549.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL038W; YAL038W; YAL038W.
GeneID851193.
KEGGsce:YAL038W.

Organism-specific databases

CYGDYAL038w.
SGDS000000036. CDC19.

Phylogenomic databases

eggNOGCOG0469.
GeneTreeENSGT00390000008859.
HOGENOMHOG000021559.
KOK00873.
OMANNKGVNF.
OrthoDBEOG7M6DJC.

Enzyme and pathway databases

BioCycYEAST:YAL038W-MONOMER.
SABIO-RKP00549.
UniPathwayUPA00109; UER00188.

Gene expression databases

GenevestigatorP00549.

Family and domain databases

Gene3D2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERPTHR11817. PTHR11817. 1 hit.
PfamPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
SUPFAMSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00549.
NextBio968037.

Entry information

Entry nameKPYK1_YEAST
AccessionPrimary (citable) accession number: P00549
Secondary accession number(s): D6VPH8, Q2VQG5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: March 19, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways