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Q9WY51 (KPYK_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate kinase

Short name=PK
EC=2.7.1.40
Gene names
Name:pyk
Ordered Locus Names:TM_0208
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Divalent metal cations. Ref.2

Enzyme regulation

Allosterically activated by AMP and inhibited by ATP.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.

Subunit structure

Homotetramer. Ref.2

Sequence similarities

Belongs to the pyruvate kinase family.

Biophysicochemical properties

Kinetic parameters:

Vmax=578 µmol/min/mg enzyme (at 65 degrees Celsius) Ref.2

pH dependence:

Optimum pH is 5.9-6.0.

Temperature dependence:

Optimum temperature is 80 degrees Celsius for the recombinant enzyme. Thermostable up to 85 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Pyruvate kinase
PRO_0000295179

Sites

Metal binding341Potassium By similarity
Metal binding361Potassium By similarity
Metal binding661Potassium By similarity
Metal binding2191Magnesium By similarity
Metal binding2431Magnesium By similarity
Binding site321Substrate By similarity
Binding site2421Substrate; via amide nitrogen By similarity
Binding site2431Substrate; via amide nitrogen By similarity
Binding site2751Substrate By similarity
Site2171Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9WY51 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 5083B7B28A5D8DEF

FASTA46651,892
        10         20         30         40         50         60 
MRSTKIVCTV GPRTDSYEMI EKMIDLGVNV FRINTSHGDW NEQEQKILKI KDLREKKKKP 

        70         80         90        100        110        120 
VAILIDLAGP KIRTGYLEKE FVELKEGQIF TLTTKEILGN EHIVSVNLSS LPKDVKKGDT 

       130        140        150        160        170        180 
ILLSDGEIVL EVIETTDTEV KTVVKVGGKI THRRGVNVPT ADLSVESITD RDREFIKLGT 

       190        200        210        220        230        240 
LHDVEFFALS FVRKPEDVLK AKEEIRKHGK EIPVISKIET KKALERLEEI IKVSDGIMVA 

       250        260        270        280        290        300 
RGDLGVEIPI EEVPIVQKEI IKLSKYYSKP VIVATQILES MIENPFPTRA EVTDIANAIF 

       310        320        330        340        350        360 
DGADALLLTA ETAVGKHPLE AIKVLSKVAK EAEKKLEFFR TIEYDTSDIS EAISHACWQL 

       370        380        390        400        410        420 
SESLNAKLII TPTISGSTAV RVSKYNVSQP IVALTPEEKT YYRLSLVRKV IPVLAEKCSQ 

       430        440        450        460 
ELEFIEKGLK KVEEMGLAEK GDLVVLTSGV PGKVGTTNTI RVLKVD 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Comparative analysis of pyruvate kinases from the hyperthermophilic archaea Archaeoglobus fulgidus, Aeropyrum pernix, and Pyrobaculum aerophilum and the hyperthermophilic bacterium Thermotoga maritima: unusual regulatory properties in hyperthermophilic archaea."
Johnsen U., Hansen T., Schoenheit P.
J. Biol. Chem. 278:25417-25427(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, REGULATION.
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD35300.1.
PIRB72406.
RefSeqNP_228023.1. NC_000853.1.
YP_007976557.1. NC_021214.1.
YP_008990818.1. NC_023151.1.

3D structure databases

ProteinModelPortalQ9WY51.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35300; AAD35300; TM_0208.
GeneID897079.
KEGGtma:TM0208.
tmi:THEMA_03685.
tmm:Tmari_0206.
PATRIC23935288. VBITheMar51294_0210.

Phylogenomic databases

eggNOGCOG0469.
KOK00873.
OMAGTHEEHK.
OrthoDBEOG6GBMB0.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-4887.
TMAR243274:GC6P-221-MONOMER.
UniPathwayUPA00109; UER00188.

Family and domain databases

Gene3D2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProIPR001697. 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]
PANTHERPTHR11817. PTHR11817. 1 hit.
PfamPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
SUPFAMSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKPYK_THEMA
AccessionPrimary (citable) accession number: Q9WY51
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways