Pyruvate kinase 1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P00549 (KPYK1_YEAST)

Last modified June 16, 2009. Version 106. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Pyruvate kinase 1
      Short name=PK 1
    EC=2.7.1.40

Gene names

Name:	PYK1
Synonyms:	CDC19
Ordered Locus Names:	YAL038W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. Ref.6
Sequence similarities	Belongs to the pyruvate kinase family.

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Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Pyruvate
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from mutant phenotype. Source: SGD pyruvate metabolic process Inferred from mutant phenotype. Source: SGD
Cellular component	plasma membrane enriched fraction Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW potassium ion binding Inferred from electronic annotation. Source: InterPro pyruvate kinase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 500

500

Pyruvate kinase 1

PRO_0000112121

Sites

Active site

240

By similarity

Metal binding

242

Magnesium Potential

Metal binding

263

Magnesium Potential

Metal binding

264

Magnesium Potential

Binding site

337

ADP Potential

Amino acid modifications

Modified residue

Phosphothreonine Ref.9 Ref.11

Modified residue

Phosphoserine Ref.9 Ref.11 Ref.7 Ref.8 Ref.10

Modified residue

Phosphoserine Ref.11

Modified residue

Phosphothreonine Ref.10

Modified residue

Phosphoserine Ref.11 Ref.7 Ref.8 Ref.10

Modified residue

Phosphothreonine Ref.11

Modified residue

Phosphoserine Ref.9 Ref.11

Modified residue

Phosphoserine Ref.9

Modified residue

213

Phosphoserine Ref.9

Modified residue

332

Phosphoserine Ref.11

Modified residue

372

Phosphothreonine Ref.7

Modified residue

402

Phosphoserine Ref.11 Ref.7

Modified residue

403

Phosphothreonine Ref.11

Modified residue

407

Phosphothreonine Ref.11

Modified residue

450

Phosphoserine Ref.11

Modified residue

478

Phosphothreonine Ref.11 Ref.7 Ref.8

Modified residue

479

Phosphotyrosine Ref.11

Modified residue

498

Phosphoserine Ref.7

Experimental info

Sequence conflict

382 – 386

VAASA → SLPR in CAA24631. Ref.1

Secondary structure

500

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P00549-1 [UniParc].

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

FASTA

500

54,545

        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

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References

	« Hide 'large scale' referencesShow '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: 2653861] [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: 6185493] [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: 16879422] [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: 7731988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	"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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-22; THR-372; SER-402; THR-478 AND SER-498, MASS SPECTROMETRY.
[8]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-22 AND THR-478, MASS SPECTROMETRY.
[9]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-9; SER-53; SER-56 AND SER-213, MASS SPECTROMETRY.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; THR-21 AND SER-22, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: 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, MASS SPECTROMETRY.
[12]	"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: 9519410] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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.

PIR

KIBYP. S05764.

RefSeq

NP_009362.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A3W	X-ray	3.00	A/B	1-500	[»]
1A3X	X-ray	3.00	A/B	1-500	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4124N.

IntAct

P00549. 186 interactions.

2-D gel databases

COMPLUYEAST-2DPAGE

P00549.

Proteomic databases

PeptideAtlas

P00549.

PRIDE

P00549.

Genome annotation databases

Ensembl

YAL038W. Saccharomyces cerevisiae. [Contig view]

GeneID

851193.

GenomeReviews

Gene locus YAL038W in contig U00091_GR.

KEGG

sce:YAL038W.

NMPDR

fig|4932.3.peg.39.

Organism-specific databases

CYGD

YAL038w.

SGD

S000000036. CDC19.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P00549.

OMA

P00549. TMENAVE.

Enzyme and pathway databases

BRENDA

2.7.1.40. 250.

Gene expression databases

ArrayExpress

P00549.

GermOnline

YAL038W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
[Graphical view]

Gene3D

G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
G3DSA:3.40.1380.20. Pyrv_Knase_a/b. 1 hit.

PANTHER

PTHR11817. Pyruvate_kinase. 1 hit.

Pfam

PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]

PRINTS

PR01050. PYRUVTKNASE.

ProDom

PD001009. Pyruvate_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01064. pyruv_kin. 1 hit.

PROSITE

PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

968037.

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Entry information

Entry name

KPYK1_YEAST

Accession

Primary (citable) accession number: P00549
Secondary accession number(s): Q2VQG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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