Pyruvate kinase 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P00549 (KPYK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 143. History...

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

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from mutant phenotype PubMed 323230. Source: SGD pyruvate metabolic process Inferred from mutant phenotype PubMed 323230. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 14718557. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro potassium ion binding Inferred from electronic annotation. Source: InterPro pyruvate kinase activity Inferred from direct assay PubMed 12063246. Source: SGD
Complete GO annotation...

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

Metal binding

Potassium By similarity

Metal binding

Potassium By similarity

Metal binding

Potassium By similarity

Metal binding

Potassium; via carbonyl oxygen By similarity

Metal binding

242

Magnesium Potential

Metal binding

266

Magnesium By similarity

Binding site

Substrate By similarity

Binding site

265

Substrate; via amide nitrogen By similarity

Binding site

266

Substrate; via amide nitrogen By similarity

Binding site

298

Substrate By similarity

Binding site

337

ADP Potential

Site

240

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

Phosphothreonine Ref.10 Ref.12

Modified residue

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphothreonine Ref.11

Modified residue

Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12

Modified residue

Phosphothreonine Ref.12

Modified residue

Phosphoserine Ref.10 Ref.12

Modified residue

Phosphoserine Ref.10

Modified residue

213

Phosphoserine Ref.10

Modified residue

332

Phosphoserine Ref.12

Modified residue

372

Phosphothreonine Ref.8

Modified residue

402

Phosphoserine Ref.8 Ref.12

Modified residue

403

Phosphothreonine Ref.12

Modified residue

407

Phosphothreonine Ref.12

Modified residue

450

Phosphoserine Ref.12

Modified residue

478

Phosphothreonine Ref.8 Ref.9 Ref.12

Modified residue

479

Phosphotyrosine Ref.12

Modified residue

498

Phosphoserine Ref.8

Experimental info

Sequence conflict

382 – 386

VAASA → SLPR in CAA24631. Ref.1

Secondary structure

500

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00549 [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

« Hide

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] [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 204511 / S288c / AB972.
[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. 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-22; THR-372; SER-402; THR-478 AND SER-498, MASS SPECTROMETRY. 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; SER-22 AND THR-478, MASS SPECTROMETRY. 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-9; SER-53; SER-56 AND SER-213, MASS SPECTROMETRY.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; THR-21 AND SER-22, MASS SPECTROMETRY.
[12]	"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 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.
[13]	"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.

PIR

KIBYP. S05764.

RefSeq

NP_009362.1. NM_001178183.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P00549.

SMR

P00549. Positions 2-500.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4124N.

IntAct

P00549. 179 interactions.

MINT

MINT-565419.

STRING

4932.YAL038W.

2D gel databases

COMPLUYEAST-2DPAGE

P00549.

Proteomic databases

PaxDb

P00549.

PeptideAtlas

P00549.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YAL038W; YAL038W; YAL038W.

GeneID

851193.

KEGG

sce:YAL038W.

Organism-specific databases

CYGD

YAL038w.

SGD

S000000036. CDC19.

Phylogenomic databases

eggNOG

COG0469.

GeneTree

ENSGT00390000008859.

HOGENOM

HOG000021559.

K00873.

OMA

NSGYTAR.

OrthoDB

EOG43XZC1.

Enzyme and pathway databases

SABIO-RK

P00549.

UniPathway

UPA00109; UER00188.

Gene expression databases

Genevestigator

P00549.

GermOnline

YAL038W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.

InterPro

IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase.
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]

PANTHER

PTHR11817. PTHR11817. 1 hit.

Pfam

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

PRINTS

PR01050. PYRUVTKNASE.

SUPFAM

SSF50800. PK_B_barrel_like. 1 hit.
SSF52935. Pyruvate_kinase. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.

TIGRFAMs

TIGR01064. pyruv_kin. 1 hit.

PROSITE

PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00549.

NextBio

968037.

Entry information

Entry name

KPYK1_YEAST

Accession

Primary (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:	April 3, 2013
This is version 143 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome I

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents