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Protein

Pyruvate kinase

Gene

pyk

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the phosphoryl transfer from phosphoenolpyruvate (PEP) to ADP to form pyruvate and ATP (PubMed:3711058, PubMed:15749828). Has a broad specificity for nucleoside diphosphates and can use ADP, GDP, IDP and UDP (PubMed:3711058).2 Publications

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Mg2+1 PublicationNote: Can also use manganese or cobalt.1 Publication
  • K+1 PublicationNote: Can also use ammonium ions.1 Publication

Enzyme regulationi

Exhibits homotropic positive cooperativity for PEP (PubMed:3711058). Allosterically activated by ribose-5-phosphate, AMP and other nucleoside monophosphates but not by fructose-1,6-bisphosphate (PubMed:3711058).1 Publication

Kineticsi

kcat is 3,204 sec(-1) (in the presence of 0.1 mM ribose-5-phosphate).1 Publication
  1. KM=0.186 mM for PEP (in the presence of 0.1 mM ribose-5-phosphate)1 Publication

    pH dependencei

    Optimum pH is 7.2 at 30 degrees Celsius. Optimum pH is 6.8 at 60 degrees Celsius.1 Publication

    Pathwayi: glycolysis

    This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.Curated
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Glyceraldehyde-3-phosphate dehydrogenase (gap)
    2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
    3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI_1)
    4. Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno)
    5. Pyruvate kinase (pyk), Pyruvate kinase (AA904_05055), Pyruvate kinase (pyk), Pyruvate kinase (GS458_2521), Pyruvate kinase (B4114_2369), Pyruvate kinase (GT94_09925)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei33SubstrateBy similarity1
    Metal bindingi35PotassiumBy similarity1
    Metal bindingi37PotassiumBy similarity1
    Metal bindingi67PotassiumBy similarity1
    Metal bindingi68Potassium; via carbonyl oxygenBy similarity1
    Binding sitei221Substrate; via amide nitrogenBy similarity1
    Sitei221Transition state stabilizerBy similarity1 Publication1
    Metal bindingi223MagnesiumBy similarity1
    Binding sitei246Substrate; via amide nitrogenBy similarity1
    Metal bindingi247MagnesiumBy similarity1
    Binding sitei247Substrate; via amide nitrogenBy similarity1
    Binding sitei279SubstrateBy similarity1

    GO - Molecular functioni

    Keywordsi

    Molecular functionAllosteric enzyme, Kinase, Transferase
    Biological processGlycolysis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

    Enzyme and pathway databases

    BRENDAi2.7.1.40 623
    UniPathwayiUPA00109; UER00188

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate kinase1 Publication (EC:2.7.1.402 Publications)
    Short name:
    PKCurated
    Alternative name(s):
    ATP:pyruvate 2-O-phosphotransferase1 Publication
    Gene namesi
    Name:pyk
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi9C → S: Slight decrease in activity; when associated with S-268. 1 Publication1
    Mutagenesisi221K → C, D, L or R: 10000 to 100000-fold decrease in activity. 1 Publication1
    Mutagenesisi268C → S: Slight decrease in activity; when associated with S-9. 1 Publication1
    Mutagenesisi308D → E: Reduced activity; when associated with Y-416. 1 Publication1
    Mutagenesisi416W → Y: Increased activity. 1 Publication1
    Mutagenesisi425H → A: Decreases affinity for allosteric activators. 1 Publication1
    Mutagenesisi435V → E, K or R: Does not affect kinetic properties. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001120551 – 587Pyruvate kinaseAdd BLAST587

    Post-translational modificationi

    The N-terminus is blocked.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Structurei

    Secondary structure

    1587
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 10Combined sources6
    Turni13 – 15Combined sources3
    Helixi18 – 27Combined sources10
    Beta strandi29 – 35Combined sources7
    Helixi41 – 57Combined sources17
    Beta strandi63 – 67Combined sources5
    Beta strandi90 – 96Combined sources7
    Beta strandi102 – 108Combined sources7
    Turni113 – 115Combined sources3
    Beta strandi121 – 124Combined sources4
    Turni125 – 128Combined sources4
    Beta strandi129 – 137Combined sources9
    Turni138 – 141Combined sources4
    Beta strandi142 – 146Combined sources5
    Beta strandi158 – 160Combined sources3
    Helixi173 – 185Combined sources13
    Beta strandi188 – 194Combined sources7
    Helixi198 – 210Combined sources13
    Beta strandi216 – 222Combined sources7
    Helixi225 – 229Combined sources5
    Helixi231 – 237Combined sources7
    Beta strandi238 – 244Combined sources7
    Helixi245 – 251Combined sources7
    Helixi254 – 256Combined sources3
    Helixi257 – 271Combined sources15
    Beta strandi275 – 282Combined sources8
    Helixi283 – 286Combined sources4
    Helixi293 – 305Combined sources13
    Beta strandi308 – 313Combined sources6
    Helixi314 – 317Combined sources4
    Helixi322 – 337Combined sources16
    Helixi342 – 350Combined sources9
    Helixi357 – 371Combined sources15
    Beta strandi375 – 380Combined sources6
    Beta strandi382 – 384Combined sources3
    Helixi385 – 392Combined sources8
    Beta strandi399 – 405Combined sources7
    Helixi406 – 411Combined sources6
    Helixi412 – 414Combined sources3
    Beta strandi418 – 422Combined sources5
    Helixi429 – 443Combined sources15
    Beta strandi451 – 456Combined sources6
    Beta strandi468 – 473Combined sources6
    Beta strandi477 – 480Combined sources4
    Beta strandi482 – 486Combined sources5
    Beta strandi492 – 495Combined sources4
    Helixi499 – 505Combined sources7
    Beta strandi511 – 515Combined sources5
    Helixi519 – 521Combined sources3
    Helixi522 – 525Combined sources4
    Beta strandi529 – 535Combined sources7
    Helixi541 – 549Combined sources9
    Beta strandi553 – 555Combined sources3
    Helixi560 – 563Combined sources4
    Beta strandi569 – 573Combined sources5
    Turni574 – 577Combined sources4
    Beta strandi578 – 582Combined sources5

    3D structure databases

    ProteinModelPortaliQ02499
    SMRiQ02499
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02499

    Family & Domainsi

    Domaini

    Contains an extra C-terminal sequence (ECTS), which contains a highly conserved PEP binding motif.1 Publication

    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

    CDDicd00288 Pyruvate_Kinase, 1 hit
    Gene3Di2.40.33.10, 1 hit
    3.40.1380.20, 1 hit
    InterProiView protein in InterPro
    IPR008279 PEP-util_enz_mobile_dom
    IPR036637 Phosphohistidine_dom_sf
    IPR001697 Pyr_Knase
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
    IPR011037 Pyrv_Knase-like_insert_dom_sf
    IPR018209 Pyrv_Knase_AS
    IPR015793 Pyrv_Knase_brl
    IPR015795 Pyrv_Knase_C
    IPR036918 Pyrv_Knase_C_sf
    IPR015806 Pyrv_Knase_insert_dom_sf
    PANTHERiPTHR11817 PTHR11817, 1 hit
    PfamiView protein in Pfam
    PF00391 PEP-utilizers, 1 hit
    PF00224 PK, 1 hit
    PF02887 PK_C, 1 hit
    PRINTSiPR01050 PYRUVTKNASE
    SUPFAMiSSF50800 SSF50800, 1 hit
    SSF51621 SSF51621, 2 hits
    SSF52009 SSF52009, 1 hit
    SSF52935 SSF52935, 1 hit
    TIGRFAMsiTIGR01064 pyruv_kin, 1 hit
    PROSITEiView protein in PROSITE
    PS00110 PYRUVATE_KINASE, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q02499-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKRKTKIVCT IGPASESVDK LVQLMEAGMN VARLNFSHGD HEEHGRRIAN
    60 70 80 90 100
    IREAAKRTGR TVAILLDTKG PEIRTHNMEN GAIELKEGSK LVISMSEVLG
    110 120 130 140 150
    TPEKISVTYP SLIDDVSVGA KILLDDGLIS LEVNAVDKQA GEIVTTVLNG
    160 170 180 190 200
    GVLKNKKGVN VPGVKVNLPG ITEKDRADIL FGIRQGIDFI AASFVRRASD
    210 220 230 240 250
    VLEIRELLEA HDALHIQIIA KIENEEGVAN IDEILEAADG LMVARGDLGV
    260 270 280 290 300
    EIPAEEVPLI QKLLIKKCNM LGKPVITATQ MLDSMQRNPR PTRAEASDVA
    310 320 330 340 350
    NAIFDGTDAV MLSGETAAGQ YPVEAVKTMH QIALRTEQAL EHRDILSQRT
    360 370 380 390 400
    KESQTTITDA IGQSVAHTAL NLDVAAIVTP TVSGKTPQMV AKYRPKAPII
    410 420 430 440 450
    AVTSNEAVSR RLALVWGVYT KEAPHVNTTD EMLDVAVDAA VRSGLVKHGD
    460 470 480 490 500
    LVVITAGVPV GETGSTNLMK VHVISDLLAK GQGIGRKSAF GKAVVAKTAE
    510 520 530 540 550
    EARQKMVDGG ILVTVSTDAD MMPAIEKAAA IITEEGGLTS HAAVVGLSLG
    560 570 580
    IPVIVGVENA TTLFKDGQEI TVDGGFGAVY RGHASVL
    Length:587
    Mass (Da):62,318
    Last modified:October 1, 1994 - v2
    Checksum:i0794BA1A07BE0D5A
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D13095 Genomic DNA Translation: BAA02406.1
    X57859 Genomic DNA Translation: CAA40994.1 Frameshift.
    PIRiS27330
    S29783
    RefSeqiWP_033014443.1, NZ_LUCR01000070.1

    Similar proteinsi

    Entry informationi

    Entry nameiKPYK_GEOSE
    AccessioniPrimary (citable) accession number: Q02499
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: October 1, 1994
    Last modified: February 28, 2018
    This is version 118 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, 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

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