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Q27686 (KPYK_LEIME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
Short name=PK
EC=2.7.1.40
Gene names
Name:PYK
OrganismLeishmania mexicana
Taxonomic identifier5665 [NCBI]
Taxonomic lineageEukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmaniinae › Leishmania ›

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium.

Potassium.

Enzyme regulation

Activated by fructose 2,6-bisphosphate, activated by the effector in a non cooperative manner.

Pathway

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

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the pyruvate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Potassium
Pyruvate
   Molecular functionKinase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionATP 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 electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Pyruvate kinase
PRO_0000112102

Sites

Metal binding521Potassium By similarity
Metal binding541Potassium By similarity
Metal binding841Potassium By similarity
Metal binding851Potassium; via carbonyl oxygen By similarity
Metal binding2411Magnesium By similarity
Metal binding2651Magnesium By similarity
Binding site501Substrate By similarity
Binding site2641Substrate; via amide nitrogen By similarity
Binding site2651Substrate; via amide nitrogen By similarity
Binding site2971Substrate By similarity
Site2391Transition state stabilizer

Secondary structure

1 .............................................................................................. 499
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q27686 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 7B8CB0F9D3EDEBA9

FASTA49954,405
        10         20         30         40         50         60 
MSQLAHNLTL SIFDPVANYR AARIICTIGP STQSVEALKG LIQSGMSVAR MNFSHGSHEY 

        70         80         90        100        110        120 
HQTTINNVRQ AAAELGVNIA IALDTKGPEI RTGQFVGGDA VMERGATCYV TTDPAFADKG 

       130        140        150        160        170        180 
TKDKFYIDYQ NLSKVVRPGN YIYIDDGILI LQVQSHEDEQ TLECTVTNSH TISDRRGVNL 

       190        200        210        220        230        240 
PGCDVDLPAV SAKDRVDLQF GVEQGVDMIF ASFIRSAEQV GDVRKALGPK GRDIMIICKI 

       250        260        270        280        290        300 
ENHQGVQNID SIIEESDGIM VARGDLGVEI PAEKVVVAQK ILISKCNVAG KPVICATQML 

       310        320        330        340        350        360 
ESMTYNPRPT RAEVSDVANA VFNGADCVML SGETAKGKYP NEVVQYMARI CLEAQSALNE 

       370        380        390        400        410        420 
YVFFNSIKKL QHIPMSADEA VCSSAVNSVY ETKAKAMVVL SNTGRSARLV AKYRPNCPIV 

       430        440        450        460        470        480 
CVTTRLQTCR QLNITQGVES VFFDADKLGH DEGKEHRVAA GVEFAKSKGY VQTGDYCVVI 

       490 
HADHKVKGYA NQTRILLVE

« Hide

References

[1]"Pyruvate kinase of Leishmania mexicana mexicana. Cloning and analysis of the gene, overexpression in Escherichia coli and characterization of the enzyme."
Ernest I., Callens M., Opperdoes F.R., Michels P.A.M.
Mol. Biochem. Parasitol. 64:43-54(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Michels P.A.M.
Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO SER-383; TYR-390; ARG-405 AND SER-406.
[3]"The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity."
Rigden D.J., Phillips S.E.V., Michels P.A.M., Fothergill-Gilmore L.A.
J. Mol. Biol. 291:615-635(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
Strain: MHOM/BZ/84/BEL46.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X74944 Genomic DNA. Translation: CAA52898.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PKLX-ray2.35A/B/C/D/E/F/G/H1-499[»]
3E0VX-ray3.30A/B/C/D/E/F1-499[»]
3E0WX-ray3.10A1-499[»]
3HQNX-ray2.00A/D1-499[»]
3HQOX-ray3.40A/B/C/K1-499[»]
3HQPX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-499[»]
3HQQX-ray5.07A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-499[»]
3IS4X-ray2.10A/B1-499[»]
3KTXX-ray2.10A/B1-499[»]
3PP7X-ray2.35A/B2-499[»]
3QV6X-ray2.85A/D1-499[»]
3QV7X-ray2.70A/B/C/D1-499[»]
3QV8X-ray2.45A/D1-499[»]
3SRKX-ray2.65A/B1-499[»]
ProteinModelPortalQ27686.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00188.

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.
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. PK_B_barrel_like. 1 hit.
SSF52935. Pyruvate_kinase. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ27686.
ChEMBLCHEMBL5149.
EvolutionaryTraceQ27686.

Entry information

Entry nameKPYK_LEIME
AccessionPrimary (citable) accession number: Q27686
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 5, 2010
Last modified: April 3, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

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

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