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Q9YEU2 (KPYK_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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:APE_0489
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length458 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=53 µmol/min/mg enzyme (at 65 degrees Celsius) Ref.2

pH dependence:

Optimum pH is 6.1.

Temperature dependence:

Optimum temperature is higher than 95 degrees Celsius. Still active after 120 minutes at 100 degrees Celsius.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458Pyruvate kinase
PRO_0000295180

Sites

Metal binding351Potassium By similarity
Metal binding371Potassium By similarity
Metal binding671Potassium By similarity
Metal binding2141Magnesium By similarity
Metal binding2381Magnesium By similarity
Binding site331Substrate By similarity
Binding site2371Substrate; via amide nitrogen By similarity
Binding site2381Substrate; via amide nitrogen By similarity
Binding site2701Substrate By similarity
Site2121Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YEU2 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 3D8E11A37A0088E3

FASTA45850,487
        10         20         30         40         50         60 
MRGPVKIVAT VGPSSSSASI LAQMLSLGVD VARINASHGG VEQWNSMLES LRRAEEAVGK 

        70         80         90        100        110        120 
RVGVAVDLEG PRVRTGNSEP VKLEKGDLVT LGFMEGDVPV DARQFFETID EGDIVLLDDG 

       130        140        150        160        170        180 
KIILQVESVE GFRVKARVLE GGVLGPRKGV VVRGKEPDLP PLSAKDRRAL EFFADKGVSH 

       190        200        210        220        230        240 
VYVSFARSAE HVEKVRTVVR RLGLRQARIF AKIEGPSGVS RIGEIAEASD GVIIARGDLG 

       250        260        270        280        290        300 
MHYSLEELPE IQELIVWEAR KRYKTVVLAT EFLSSMIEKP VPTRSEVVDI YQAVLQTADA 

       310        320        330        340        350        360 
LMLTGETAIG KYPVKSVQWM AKISSRAYKK LATSPPERPR PTSTPYKLAL GLVELAESLD 

       370        380        390        400        410        420 
SPLVVYSKTG RFAERLASFK PLKTFYVGVP SREVERVVRH LWGAEPIVVG DYPYEAGLAK 

       430        440        450 
TYEKLRRENI IHGDETVVEA AWSSERGIYI IRVRNLEF 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1."
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. expand/collapse author list , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.
DNA Res. 6:83-101(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.
[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 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA79454.1.
PIRB72745.
RefSeqNP_147274.1. NC_000854.2.

3D structure databases

ProteinModelPortalQ9YEU2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272557.APE_0489.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA79454; BAA79454; APE_0489.
GeneID1444673.
KEGGape:APE_0489.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0469.
HOGENOMHOG000021558.
KOK00873.
OMAQRPEDIH.
ProtClustDBCLSK2747737.

Enzyme and pathway databases

BioCycAPER272557:GJD6-377-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_AERPE
AccessionPrimary (citable) accession number: Q9YEU2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: November 1, 1999
Last modified: February 19, 2014
This is version 73 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