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Q27686

- KPYK_LEIME

UniProt

Q27686 - KPYK_LEIME

Protein

Pyruvate kinase

Gene

PYK

Organism
Leishmania mexicana
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    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 – 501SubstrateBy similarity
    Metal bindingi52 – 521PotassiumBy similarity
    Metal bindingi54 – 541PotassiumBy similarity
    Metal bindingi84 – 841PotassiumBy similarity
    Metal bindingi85 – 851Potassium; via carbonyl oxygenBy similarity
    Sitei239 – 2391Transition state stabilizer
    Metal bindingi241 – 2411MagnesiumBy similarity
    Binding sitei264 – 2641Substrate; via amide nitrogenBy similarity
    Metal bindingi265 – 2651MagnesiumBy similarity
    Binding sitei265 – 2651Substrate; via amide nitrogenBy similarity
    Binding sitei297 – 2971SubstrateBy 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

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-UniPathway

    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 kinasePRO_0000112102Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    499
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ27686.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pyruvate kinase family.Curated

    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...
    MobiDBi 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: October 1, 2014
    This is version 90 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