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Q8ZYE0 (KPYK_PYRAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:PAE0819
OrganismPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827) [Reference proteome] [HAMAP]
Taxonomic identifier178306 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Pyrobaculum ›

Protein attributes

Sequence length461 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

Not activated by classical allosteric effectors.

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=46 µmol/min/mg enzyme (at 65 degrees Celsius) Ref.2

pH dependence:

Optimum pH is 6.0.

Temperature dependence:

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Pyruvate kinase
PRO_0000295181

Sites

Metal binding481Potassium By similarity
Metal binding801Potassium By similarity
Metal binding2321Magnesium By similarity
Metal binding2561Magnesium By similarity
Binding site461Substrate By similarity
Binding site2551Substrate; via amide nitrogen By similarity
Binding site2561Substrate; via amide nitrogen By similarity
Binding site2881Substrate By similarity
Site2301Transition state stabilizer By similarity

Secondary structure

1 ................................................................................... 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8ZYE0 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: D43333DA69BDE14C

FASTA46150,262
        10         20         30         40         50         60 
MSAPRGDHAI LRARNLTKRV ATLGPSTDVL RPDELIKFLD LVDGVRINLA HASPNEVKFR 

        70         80         90        100        110        120 
IEAVRSYEKA KNRPLAVIVD LKGPSIRVGS TSPINVQEGE VVKFKLSDKS DGTYIPVPNK 

       130        140        150        160        170        180 
AFFSAVEQND VILMLDGRLR LKVTNTGSDW IEAVAESSGV ITGGKAIVVE GKDYDISTPA 

       190        200        210        220        230        240 
EEDVEALKAI SPIRDNIDYV AISLAKSCKD VDSVRSLLTE LGFQSQVAVK IETKGAVNNL 

       250        260        270        280        290        300 
EELVQCSDYV VVARGDLGLH YGLDALPIVQ RRIVHTSLKY GKPIAVATQL LDSMQSSPIP 

       310        320        330        340        350        360 
TRAEINDVFT TASMGVDSLW LTNETASGKY PLAAVSWLSR ILMNVEYQIP QSPLLQNSRD 

       370        380        390        400        410        420 
RFAKGLVELA QDLGANILVF SMSGTLARRI AKFRPRGVVY VGTPNVRVAR SLSIVWALEP 

       430        440        450        460 
LYIPAENYEE GLEKLISLKG TTPFVATYGI RGGVHSVKVK L

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.
[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 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE009441 Genomic DNA. Translation: AAL63053.1.
RefSeqNP_558871.1. NC_003364.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QTGX-ray2.20A/B1-461[»]
ProteinModelPortalQ8ZYE0.
ModBaseSearch...

Protein-protein interaction databases

STRING178306.PAE0819.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL63053; AAL63053; PAE0819.
GeneID1465282.
KEGGpai:PAE0819.

Phylogenomic databases

eggNOGCOG0469.
HOGENOMHOG000021558.
KOK00873.
OMAALHRIGT.
ProtClustDBCLSK631371.

Enzyme and pathway databases

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.
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. PK_B_barrel_like. 1 hit.
SSF52935. Pyruvate_kinase. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKPYK_PYRAE
AccessionPrimary (citable) accession number: Q8ZYE0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: March 1, 2002
Last modified: May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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