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Q27686

- KPYK_LEIME

UniProt

Q27686 - KPYK_LEIME

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Protein
Pyruvate kinase
Gene
PYK
Organism
Leishmania mexicana
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Magnesium.
Potassium.

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501Substrate By similarity
Metal bindingi52 – 521Potassium By similarity
Metal bindingi54 – 541Potassium By similarity
Metal bindingi84 – 841Potassium By similarity
Metal bindingi85 – 851Potassium; via carbonyl oxygen By similarity
Sitei239 – 2391Transition state stabilizer
Metal bindingi241 – 2411Magnesium By similarity
Binding sitei264 – 2641Substrate; via amide nitrogen By similarity
Metal bindingi265 – 2651Magnesium By similarity
Binding sitei265 – 2651Substrate; via amide nitrogen By similarity
Binding sitei297 – 2971Substrate By similarity

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: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
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

UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
Gene namesi
Name:PYK
OrganismiLeishmania mexicana
Taxonomic identifieri5665 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Pyruvate kinase
PRO_0000112102Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 86
Beta strandi18 – 203
Beta strandi22 – 298
Turni30 – 323
Helixi35 – 4410
Beta strandi46 – 527
Helixi58 – 7518
Beta strandi80 – 845
Beta strandi90 – 923
Helixi96 – 983
Beta strandi99 – 1024
Beta strandi107 – 1115
Helixi114 – 1163
Beta strandi117 – 1204
Beta strandi122 – 1287
Helixi132 – 1354
Beta strandi141 – 1444
Turni145 – 1484
Beta strandi149 – 15810
Beta strandi161 – 1666
Beta strandi170 – 1734
Beta strandi177 – 1793
Helixi192 – 20312
Beta strandi207 – 2115
Helixi217 – 22711
Helixi229 – 2313
Beta strandi234 – 2407
Helixi243 – 2475
Helixi249 – 2557
Beta strandi256 – 2627
Helixi263 – 2697
Helixi272 – 28918
Beta strandi293 – 3008
Helixi301 – 3044
Beta strandi306 – 3083
Helixi311 – 32313
Beta strandi326 – 3316
Helixi332 – 3354
Helixi340 – 35718
Helixi360 – 36910
Helixi377 – 39216
Beta strandi395 – 4006
Beta strandi402 – 4043
Helixi405 – 4128
Beta strandi419 – 4246
Helixi426 – 4316
Helixi432 – 4343
Beta strandi438 – 4425
Helixi445 – 4484
Helixi455 – 46713
Beta strandi476 – 4827
Beta strandi491 – 4977

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ27686.

Miscellaneous databases

EvolutionaryTraceiQ27686.

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.

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.

Q27686-1 [UniParc]FASTAAdd to Basket

« Hide

MSQLAHNLTL SIFDPVANYR AARIICTIGP STQSVEALKG LIQSGMSVAR    50
MNFSHGSHEY HQTTINNVRQ AAAELGVNIA IALDTKGPEI RTGQFVGGDA 100
VMERGATCYV TTDPAFADKG TKDKFYIDYQ NLSKVVRPGN YIYIDDGILI 150
LQVQSHEDEQ TLECTVTNSH TISDRRGVNL PGCDVDLPAV SAKDRVDLQF 200
GVEQGVDMIF ASFIRSAEQV GDVRKALGPK GRDIMIICKI ENHQGVQNID 250
SIIEESDGIM VARGDLGVEI PAEKVVVAQK ILISKCNVAG KPVICATQML 300
ESMTYNPRPT RAEVSDVANA VFNGADCVML SGETAKGKYP NEVVQYMARI 350
CLEAQSALNE YVFFNSIKKL QHIPMSADEA VCSSAVNSVY ETKAKAMVVL 400
SNTGRSARLV AKYRPNCPIV CVTTRLQTCR QLNITQGVES VFFDADKLGH 450
DEGKEHRVAA GVEFAKSKGY VQTGDYCVVI HADHKVKGYA NQTRILLVE 499
Length:499
Mass (Da):54,405
Last modified:October 5, 2010 - v2
Checksum:i7B8CB0F9D3EDEBA9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74944 Genomic DNA. Translation: CAA52898.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74944 Genomic DNA. Translation: CAA52898.2 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PKL X-ray 2.35 A/B/C/D/E/F/G/H 1-499 [» ]
3E0V X-ray 3.30 A/B/C/D/E/F 1-499 [» ]
3E0W X-ray 3.10 A 1-499 [» ]
3HQN X-ray 2.00 A/D 1-499 [» ]
3HQO X-ray 3.40 A/B/C/K 1-499 [» ]
3HQP X-ray 2.30 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 1-499 [» ]
3HQQ X-ray 5.07 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-499 [» ]
3IS4 X-ray 2.10 A/B 1-499 [» ]
3KTX X-ray 2.10 A/B 1-499 [» ]
3PP7 X-ray 2.35 A/B 2-499 [» ]
3QV6 X-ray 2.85 A/D 1-499 [» ]
3QV7 X-ray 2.70 A/B/C/D 1-499 [» ]
3QV8 X-ray 2.45 A/D 1-499 [» ]
3SRK X-ray 2.65 A/B 1-499 [» ]
ProteinModelPortali Q27686.
ModBasei Search...

Chemistry

BindingDBi Q27686.
ChEMBLi CHEMBL5149.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .

Miscellaneous databases

EvolutionaryTracei Q27686.

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProi IPR001697. 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 ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiKPYK_LEIME
AccessioniPrimary (citable) accession number: Q27686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 5, 2010
Last modified: June 11, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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