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Q02499

- KPYK_GEOSE

UniProt

Q02499 - KPYK_GEOSE

Protein

Pyruvate kinase

Gene

pyk

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + pyruvate = ADP + phosphoenolpyruvate.

    Cofactori

    Magnesium.
    Potassium.

    Enzyme regulationi

    Regulated by phosphoenolpyruvate substrate and is allosterically activated by ribose-5-phosphate, AMP and other nucleoside monophosphates but not by fructose-1,6-bisphosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331SubstrateBy similarity
    Metal bindingi35 – 351PotassiumBy similarity
    Metal bindingi37 – 371PotassiumBy similarity
    Metal bindingi67 – 671PotassiumBy similarity
    Metal bindingi68 – 681Potassium; via carbonyl oxygenBy similarity
    Sitei221 – 2211Transition state stabilizerBy similarity
    Metal bindingi223 – 2231MagnesiumBy similarity
    Binding sitei246 – 2461Substrate; via amide nitrogenBy similarity
    Metal bindingi247 – 2471MagnesiumBy similarity
    Binding sitei247 – 2471Substrate; via amide nitrogenBy similarity
    Binding sitei279 – 2791SubstrateBy 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
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi308 – 3081D → E: Reduced activity; when associated with Y-416.
    Mutagenesisi416 – 4161W → Y: Increased activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 587587Pyruvate kinasePRO_0000112055Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei541 – 5411PhosphohistidineBy similarity

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    587
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Turni13 – 153
    Helixi18 – 2710
    Beta strandi29 – 357
    Helixi41 – 5717
    Beta strandi63 – 675
    Beta strandi90 – 967
    Beta strandi102 – 1087
    Turni113 – 1153
    Beta strandi121 – 1244
    Turni125 – 1284
    Beta strandi129 – 1379
    Turni138 – 1414
    Beta strandi142 – 1465
    Beta strandi158 – 1603
    Helixi173 – 18513
    Beta strandi188 – 1947
    Helixi198 – 21013
    Beta strandi216 – 2227
    Helixi225 – 2295
    Helixi231 – 2377
    Beta strandi238 – 2447
    Helixi245 – 2517
    Helixi254 – 2563
    Helixi257 – 27115
    Beta strandi275 – 2828
    Helixi283 – 2864
    Helixi293 – 30513
    Beta strandi308 – 3136
    Helixi314 – 3174
    Helixi322 – 33716
    Helixi342 – 3509
    Helixi357 – 37115
    Beta strandi375 – 3806
    Beta strandi382 – 3843
    Helixi385 – 3928
    Beta strandi399 – 4057
    Helixi406 – 4116
    Helixi412 – 4143
    Beta strandi418 – 4225
    Helixi429 – 44315
    Beta strandi451 – 4566
    Beta strandi468 – 4736
    Beta strandi477 – 4804
    Beta strandi482 – 4865
    Beta strandi492 – 4954
    Helixi499 – 5057
    Beta strandi511 – 5155
    Helixi519 – 5213
    Helixi522 – 5254
    Beta strandi529 – 5357
    Helixi541 – 5499
    Beta strandi553 – 5553
    Helixi560 – 5634
    Beta strandi569 – 5735
    Turni574 – 5774
    Beta strandi578 – 5825

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E28X-ray2.40A1-587[»]
    ProteinModelPortaliQ02499.
    SMRiQ02499. Positions 1-587.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02499.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pyruvate kinase family.Curated
    In the C-terminal section; belongs to the PEP-utilizing enzyme family.Curated

    Family and domain databases

    Gene3Di2.40.33.10. 1 hit.
    3.20.20.60. 2 hits.
    3.40.1380.20. 1 hit.
    3.50.30.10. 1 hit.
    InterProiIPR008279. PEP-util_enz_mobile_dom.
    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]
    PANTHERiPTHR11817. PTHR11817. 1 hit.
    PfamiPF00391. PEP-utilizers. 1 hit.
    PF00224. PK. 1 hit.
    PF02887. PK_C. 1 hit.
    [Graphical view]
    PRINTSiPR01050. PYRUVTKNASE.
    SUPFAMiSSF50800. SSF50800. 1 hit.
    SSF51621. SSF51621. 2 hits.
    SSF52009. SSF52009. 1 hit.
    SSF52935. SSF52935. 1 hit.
    TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
    PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q02499-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRKTKIVCT IGPASESVDK LVQLMEAGMN VARLNFSHGD HEEHGRRIAN    50
    IREAAKRTGR TVAILLDTKG PEIRTHNMEN GAIELKEGSK LVISMSEVLG 100
    TPEKISVTYP SLIDDVSVGA KILLDDGLIS LEVNAVDKQA GEIVTTVLNG 150
    GVLKNKKGVN VPGVKVNLPG ITEKDRADIL FGIRQGIDFI AASFVRRASD 200
    VLEIRELLEA HDALHIQIIA KIENEEGVAN IDEILEAADG LMVARGDLGV 250
    EIPAEEVPLI QKLLIKKCNM LGKPVITATQ MLDSMQRNPR PTRAEASDVA 300
    NAIFDGTDAV MLSGETAAGQ YPVEAVKTMH QIALRTEQAL EHRDILSQRT 350
    KESQTTITDA IGQSVAHTAL NLDVAAIVTP TVSGKTPQMV AKYRPKAPII 400
    AVTSNEAVSR RLALVWGVYT KEAPHVNTTD EMLDVAVDAA VRSGLVKHGD 450
    LVVITAGVPV GETGSTNLMK VHVISDLLAK GQGIGRKSAF GKAVVAKTAE 500
    EARQKMVDGG ILVTVSTDAD MMPAIEKAAA IITEEGGLTS HAAVVGLSLG 550
    IPVIVGVENA TTLFKDGQEI TVDGGFGAVY RGHASVL 587
    Length:587
    Mass (Da):62,318
    Last modified:October 1, 1994 - v2
    Checksum:i0794BA1A07BE0D5A
    GO

    Sequence cautioni

    The sequence CAA40994.1 differs from that shown. Reason: Frameshift at position 486.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13095 Genomic DNA. Translation: BAA02406.1.
    X57859 Genomic DNA. Translation: CAA40994.1. Frameshift.
    PIRiS27330.
    S29783.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13095 Genomic DNA. Translation: BAA02406.1 .
    X57859 Genomic DNA. Translation: CAA40994.1 . Frameshift.
    PIRi S27330.
    S29783.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E28 X-ray 2.40 A 1-587 [» ]
    ProteinModelPortali Q02499.
    SMRi Q02499. Positions 1-587.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00188 .

    Miscellaneous databases

    EvolutionaryTracei Q02499.

    Family and domain databases

    Gene3Di 2.40.33.10. 1 hit.
    3.20.20.60. 2 hits.
    3.40.1380.20. 1 hit.
    3.50.30.10. 1 hit.
    InterProi IPR008279. PEP-util_enz_mobile_dom.
    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 PF00391. PEP-utilizers. 1 hit.
    PF00224. PK. 1 hit.
    PF02887. PK_C. 1 hit.
    [Graphical view ]
    PRINTSi PR01050. PYRUVTKNASE.
    SUPFAMi SSF50800. SSF50800. 1 hit.
    SSF51621. SSF51621. 2 hits.
    SSF52009. SSF52009. 1 hit.
    SSF52935. SSF52935. 1 hit.
    TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
    PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon."
      Sakai H., Ohta T.
      Eur. J. Biochem. 211:851-859(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 328-346 AND 393-396.
      Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
    2. "Key residues in the allosteric transition of Bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis."
      Walker D., Chia W.N., Muirhead H.
      J. Mol. Biol. 228:265-276(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-51.
      Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.

    Entry informationi

    Entry nameiKPYK_GEOSE
    AccessioniPrimary (citable) accession number: Q02499
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Direct protein sequencing

    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