Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyruvate kinase

Gene

pyk1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561SubstrateBy similarity
Metal bindingi58 – 581PotassiumBy similarity
Metal bindingi60 – 601PotassiumBy similarity
Metal bindingi91 – 911PotassiumBy similarity
Metal bindingi92 – 921Potassium; via carbonyl oxygenBy similarity
Sitei247 – 2471Transition state stabilizerBy similarity
Metal bindingi249 – 2491MagnesiumSequence Analysis
Binding sitei272 – 2721Substrate; via amide nitrogenBy similarity
Metal bindingi273 – 2731MagnesiumBy similarity
Binding sitei273 – 2731Substrate; via amide nitrogenBy similarity
Binding sitei305 – 3051SubstrateBy similarity
Binding sitei344 – 3441ADPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: PomBase

GO - Biological processi

  1. canonical glycolysis Source: PomBase
  2. cellular response to nitrogen starvation Source: PomBase
  3. negative regulation of G0 to G1 transition Source: PomBase
  4. pyruvate metabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

BRENDAi2.7.1.40. 5613.
ReactomeiREACT_288992. Regulation of gene expression in beta cells.
REACT_304275. Glycolysis.
REACT_326011. ChREBP activates metabolic gene expression.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
Gene namesi
Name:pyk1
ORF Names:SPAC4H3.10c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC4H3.10c.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 509509Pyruvate kinasePRO_0000112118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291Phosphoserine1 Publication
Modified residuei63 – 631Phosphoserine1 Publication
Modified residuei281 – 2811Phosphoserine1 Publication
Modified residuei412 – 4121Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ10208.
PaxDbiQ10208.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi279974. 7 interactions.
MINTiMINT-4697816.
STRINGi4896.SPAC4H3.10c-1.

Structurei

3D structure databases

ProteinModelPortaliQ10208.
SMRiQ10208. Positions 26-506.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
InParanoidiQ10208.
KOiK00873.
OMAiPLECATE.
OrthoDBiEOG7M6DJC.
PhylomeDBiQ10208.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. 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]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10208-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSAVSPKQ WVAGLNSELD IPAVNRRTSI ICTIGPKSNN VETLCKLRDA
60 70 80 90 100
GMNIVRMNFS HGSYEYHQSV IDNARKASAT NPLFPLAIAL DTKGPEIRTG
110 120 130 140 150
LTVGGTDYPI SSGHEMIFTT DDAYAEKCND KVMYIDYKNI TKVIQPGRII
160 170 180 190 200
YVDDGILSFT VIEKVDDKNL KVRVNNNGKI SSKKGVNLPK TDVDLPALSE
210 220 230 240 250
KDKADLRFGV KNGVDMIFAS FIRRAEDVIH IREVLGEEGK NIKIICKIEN
260 270 280 290 300
QQGVNNFDSI LDVTDGIMVA RGDLGIEIPA SQVFVAQKMM IAKCNIAGKP
310 320 330 340 350
VACATQMLES MTYNPRPTRA EVSDVGNAVL DGADLVMLSG ETTKGSYPVE
360 370 380 390 400
AVTYMAETAR VAEASIPYGS LYQEMFGLVR RPLECATETT AVAAIGASIE
410 420 430 440 450
SDAKAIVVLS TSGNTARLCS KYRPSIPIVM VTRCPQRARQ SHLNRGVYPV
460 470 480 490 500
IYEKEPLSDW QKDVDARVAY GCQQAYKMNI LKKGDKIIVL QGAVGGKGHT

SIFRLTVAE
Length:509
Mass (Da):55,515
Last modified:October 1, 1996 - v1
Checksum:i589378533FCFD5F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti391 – 3911A → R in CAA62490 (PubMed:8586271).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91008 mRNA. Translation: CAA62490.1.
CU329670 Genomic DNA. Translation: CAA93349.1.
PIRiT38890.
T45166.
RefSeqiNP_594346.1. NM_001019767.2.

Genome annotation databases

EnsemblFungiiSPAC4H3.10c.1; SPAC4H3.10c.1:pep; SPAC4H3.10c.
GeneIDi2543557.
KEGGispo:SPAC4H3.10c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91008 mRNA. Translation: CAA62490.1.
CU329670 Genomic DNA. Translation: CAA93349.1.
PIRiT38890.
T45166.
RefSeqiNP_594346.1. NM_001019767.2.

3D structure databases

ProteinModelPortaliQ10208.
SMRiQ10208. Positions 26-506.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279974. 7 interactions.
MINTiMINT-4697816.
STRINGi4896.SPAC4H3.10c-1.

Proteomic databases

MaxQBiQ10208.
PaxDbiQ10208.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC4H3.10c.1; SPAC4H3.10c.1:pep; SPAC4H3.10c.
GeneIDi2543557.
KEGGispo:SPAC4H3.10c.

Organism-specific databases

PomBaseiSPAC4H3.10c.

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
InParanoidiQ10208.
KOiK00873.
OMAiPLECATE.
OrthoDBiEOG7M6DJC.
PhylomeDBiQ10208.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
BRENDAi2.7.1.40. 5613.
ReactomeiREACT_288992. Regulation of gene expression in beta cells.
REACT_304275. Glycolysis.
REACT_326011. ChREBP activates metabolic gene expression.

Miscellaneous databases

NextBioi20804566.
PROiQ10208.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. 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]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a gene encoding pyruvate kinase from Schizosaccharomyces pombe; implications for quaternary structure and regulation of the enzyme."
    Nairn J., Smith S., Allison P.J., Rigden D., Fothergill-Gilmore L.A., Price N.C.
    FEMS Microbiol. Lett. 134:221-226(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    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.
    Nature 415:871-880(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-63; SER-281 AND SER-412, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiKPYK_SCHPO
AccessioniPrimary (citable) accession number: Q10208
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 1, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.