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Reviewed, UniProtKB/Swiss-Prot P22200 (KPYC_SOLTU)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyruvate kinase, cytosolic isozyme
      Short name=PK
    EC=2.7.1.40
OrganismSolanum tuberosum (Potato)
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium.

Potassium.

Pathway

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

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the pyruvate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Pyruvate
   Molecular functionKinase
Transferase
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP 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 electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510Pyruvate kinase, cytosolic isozyme
PRO_0000112124

Sites

Active site2401 By similarity
Metal binding2421Magnesium Potential
Metal binding2631Magnesium Potential
Metal binding2641Magnesium Potential

Natural variations

Natural variant1331M → V
Natural variant1691T → S
Natural variant2271V → A
Natural variant3091A → R

Sequences

Sequence LengthMass (Da)Tools
P22200-1 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 1752C9ED920F2854

FASTA51055,170
        10         20         30         40         50         60 
MANIDIAGIM KDLPNDGRIP KTKIVCTLGP SSRTVPMLEK LLRAGMNVAR FNFSHGTHEY 

        70         80         90        100        110        120 
HQETLDNLKI AMQNTQILCA VMLDTKGPEI RTGFLTDGKP IQLKEGQEIT VSTDYTIKGN 

       130        140        150        160        170        180 
EEMISMSYKK LVMDLKPGNT ILCADGTITL TVLSCDPPSG TVRCRCENTA TLGERKNVNL 

       190        200        210        220        230        240 
PGVVVDLPTL TEKDKEDILE WGVPNNIDMI ALSFVRKGSD LVNVRKVLGP HAKRIQLMSK 

       250        260        270        280        290        300 
VENQEGVINF DEILRETDSF MVARGDLGME IPVEKIFLAQ KMMIYKCNLA GKAVVTATQM 

       310        320        330        340        350        360 
LESMIKSPAP TRAEATDVAN AVLDGTDCVM LSGESAAGAY PELAVKIMSR ICIEAESSLD 

       370        380        390        400        410        420 
NEAIFKEMIR CTPLPMSPLE SLASSAVRTA NKARAKLIVV LTRGGSTAKL VAKYRPAVPI 

       430        440        450        460        470        480 
LSVVVPVLTT DSFDWSISDE TPARHSLVYR GLIPLLGEGS AKATDSESTE VILEAALKSA 

       490        500        510 
VTRGLCKPGD AVVALHRIGS ASVIKICVVK 

« Hide

References

[1]"Cloning and characterization of a cDNA for the cytosolic isozyme of plant pyruvate kinase: the relationship between the plant and non-plant enzyme."
Blakeley S.D., Plaxton W.C., Dennis D.T.
Plant Mol. Biol. 15:665-669(1990) [PubMed: 2102383] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Kennebec.
Tissue: Tuber.
[2]"Structure of the gene encoding potato cytosolic pyruvate kinase."
Cole K.P., Blakeley S.D., Dennis D.T.
Gene 122:255-261(1992) [PubMed: 1487141] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

X53688 mRNA. Translation: CAA37727.1.
PIRJC1481.

3D structure databases

HSSPHSSP built from PDB template 1E0T based on UniProtKB P14178.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.7.1.40. 296.

Family and domain databases

InterProIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
[Graphical view]
Gene3DG3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
G3DSA:3.40.1380.20. Pyrv_Knase_a/b. 1 hit.
PANTHERPTHR11817. Pyruvate_kinase. 1 hit.
PfamPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
ProDomPD001009. Pyruvate_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKPYC_SOLTU
AccessionPrimary (citable) accession number: P22200
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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