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Protein

Pyruvate kinase

Gene

pyk

Organism
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

a divalent metal cation1 Publication

Enzyme regulationi

Not activated by classical allosteric effectors.

Kineticsi

    1. Vmax=46 µmol/min/mg enzyme (at 65 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Temperature dependencei

    Optimum temperature is higher than 98 degrees Celsius. Thermostable for 2 hours up to 100 degrees Celsius.1 Publication

    Pathwayi: glycolysis

    This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
    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)
    3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM)
    4. Enolase (eno)
    5. Pyruvate kinase (pyk)
    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 sitei46SubstrateBy similarity1
    Metal bindingi48PotassiumBy similarity1
    Metal bindingi80PotassiumBy similarity1
    Sitei230Transition state stabilizerBy similarity1
    Metal bindingi232MagnesiumBy similarity1
    Binding sitei255Substrate; via amide nitrogenBy similarity1
    Metal bindingi256MagnesiumBy similarity1
    Binding sitei256Substrate; via amide nitrogenBy similarity1
    Binding sitei288SubstrateBy similarity1

    GO - Molecular functioni

    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

    BRENDAi2.7.1.40. 5239.
    UniPathwayiUPA00109; UER00188.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate kinase (EC:2.7.1.40)
    Short name:
    PK
    Gene namesi
    Name:pyk
    Ordered Locus Names:PAE0819
    OrganismiPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
    Taxonomic identifieri178306 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
    Proteomesi
    • UP000002439 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002951811 – 461Pyruvate kinaseAdd BLAST461

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi178306.PAE0819.

    Structurei

    Secondary structure

    1461
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi16 – 22Combined sources7
    Helixi25 – 28Combined sources4
    Helixi32 – 39Combined sources8
    Beta strandi43 – 48Combined sources6
    Turni49 – 51Combined sources3
    Helixi54 – 71Combined sources18
    Beta strandi76 – 80Combined sources5
    Beta strandi94 – 96Combined sources3
    Beta strandi101 – 106Combined sources6
    Beta strandi112 – 117Combined sources6
    Helixi120 – 125Combined sources6
    Beta strandi131 – 134Combined sources4
    Helixi135 – 137Combined sources3
    Beta strandi139 – 146Combined sources8
    Beta strandi148 – 157Combined sources10
    Beta strandi159 – 161Combined sources3
    Beta strandi166 – 169Combined sources4
    Helixi181 – 190Combined sources10
    Helixi191 – 196Combined sources6
    Beta strandi199 – 202Combined sources4
    Helixi208 – 220Combined sources13
    Beta strandi226 – 231Combined sources6
    Helixi234 – 238Combined sources5
    Helixi240 – 245Combined sources6
    Beta strandi248 – 253Combined sources6
    Helixi254 – 257Combined sources4
    Turni258 – 260Combined sources3
    Turni263 – 265Combined sources3
    Helixi266 – 279Combined sources14
    Beta strandi284 – 291Combined sources8
    Helixi292 – 295Combined sources4
    Helixi302 – 313Combined sources12
    Beta strandi317 – 321Combined sources5
    Helixi323 – 326Combined sources4
    Helixi331 – 343Combined sources13
    Helixi358 – 373Combined sources16
    Beta strandi376 – 380Combined sources5
    Beta strandi382 – 384Combined sources3
    Helixi385 – 391Combined sources7
    Beta strandi399 – 404Combined sources6
    Helixi406 – 412Combined sources7
    Beta strandi418 – 422Combined sources5
    Helixi428 – 439Combined sources12
    Beta strandi442 – 448Combined sources7
    Beta strandi456 – 460Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3QTGX-ray2.20A/B1-461[»]
    ProteinModelPortaliQ8ZYE0.
    SMRiQ8ZYE0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pyruvate kinase family.Curated

    Phylogenomic databases

    eggNOGiarCOG04120. Archaea.
    COG0469. LUCA.
    HOGENOMiHOG000021558.
    InParanoidiQ8ZYE0.
    KOiK00873.
    OMAiNMSHATT.

    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q8ZYE0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSAPRGDHAI LRARNLTKRV ATLGPSTDVL RPDELIKFLD LVDGVRINLA
    60 70 80 90 100
    HASPNEVKFR IEAVRSYEKA KNRPLAVIVD LKGPSIRVGS TSPINVQEGE
    110 120 130 140 150
    VVKFKLSDKS DGTYIPVPNK AFFSAVEQND VILMLDGRLR LKVTNTGSDW
    160 170 180 190 200
    IEAVAESSGV ITGGKAIVVE GKDYDISTPA EEDVEALKAI SPIRDNIDYV
    210 220 230 240 250
    AISLAKSCKD VDSVRSLLTE LGFQSQVAVK IETKGAVNNL EELVQCSDYV
    260 270 280 290 300
    VVARGDLGLH YGLDALPIVQ RRIVHTSLKY GKPIAVATQL LDSMQSSPIP
    310 320 330 340 350
    TRAEINDVFT TASMGVDSLW LTNETASGKY PLAAVSWLSR ILMNVEYQIP
    360 370 380 390 400
    QSPLLQNSRD RFAKGLVELA QDLGANILVF SMSGTLARRI AKFRPRGVVY
    410 420 430 440 450
    VGTPNVRVAR SLSIVWALEP LYIPAENYEE GLEKLISLKG TTPFVATYGI
    460
    RGGVHSVKVK L
    Length:461
    Mass (Da):50,262
    Last modified:March 1, 2002 - v1
    Checksum:iD43333DA69BDE14C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009441 Genomic DNA. Translation: AAL63053.1.

    Genome annotation databases

    EnsemblBacteriaiAAL63053; AAL63053; PAE0819.
    KEGGipai:PAE0819.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009441 Genomic DNA. Translation: AAL63053.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3QTGX-ray2.20A/B1-461[»]
    ProteinModelPortaliQ8ZYE0.
    SMRiQ8ZYE0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi178306.PAE0819.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL63053; AAL63053; PAE0819.
    KEGGipai:PAE0819.

    Phylogenomic databases

    eggNOGiarCOG04120. Archaea.
    COG0469. LUCA.
    HOGENOMiHOG000021558.
    InParanoidiQ8ZYE0.
    KOiK00873.
    OMAiNMSHATT.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00188.
    BRENDAi2.7.1.40. 5239.

    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.
    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.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiKPYK_PYRAE
    AccessioniPrimary (citable) accession number: Q8ZYE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: March 1, 2002
    Last modified: November 2, 2016
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.