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P00548 (KPYM_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. 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 PKM

EC=2.7.1.40
Gene names
Name:PKM
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a key role in glycolysis By similarity.

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium.

Potassium.

Enzyme regulation

Allosterically activated by fructose 1,6-bisphosphate By similarity.

Pathway

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

Subunit structure

Homotetramer.

Miscellaneous

This activity is regulated by glucose levels.

Sequence similarities

Belongs to the pyruvate kinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 530529Pyruvate kinase PKM
PRO_0000112097

Regions

Region431 – 4366Allosteric activator binding By similarity
Region515 – 5206Allosteric activator binding By similarity

Sites

Metal binding741Potassium By similarity
Metal binding761Potassium By similarity
Metal binding1121Potassium By similarity
Metal binding1131Potassium; via carbonyl oxygen By similarity
Metal binding2711Magnesium By similarity
Metal binding2951Magnesium By similarity
Binding site721Substrate By similarity
Binding site2941Substrate; via amide nitrogen By similarity
Binding site2951Substrate; via amide nitrogen By similarity
Binding site3271Substrate By similarity
Binding site4811Allosteric activator By similarity
Binding site4881Allosteric activator By similarity
Site2691Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P00548 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8B0DF09FD82EB72F

FASTA53058,015
        10         20         30         40         50         60 
MSKHHDAGTA FIQTQQLHAA MADTFLEHMC RLDIDSEPTI ARNTGIICTI GPASRSVDKL 

        70         80         90        100        110        120 
KEMIKSGMNV ARLNFSHGTH EYHEGTIKNV REATESFASD PITYRPVAIA LDTKGPEIRT 

       130        140        150        160        170        180 
GLIKGSGTAE VELKKGAALK VTLDNAFMEN CDENVLWVDY KNLIKVIDVG SKIYVDDGLI 

       190        200        210        220        230        240 
SLLVKEKGKD FVMTEVENGG MLGSKKGVNL PGAAVDLPAV SEKDIQDLKF GVEQNVDMVF 

       250        260        270        280        290        300 
ASFIRKAADV HAVRKVLGEK GKHIKIISKI ENHEGVRRFD EIMEASDGIM VARGDLGIEI 

       310        320        330        340        350        360 
PAEKVFLAQK MMIGRCNRAG KPIICATQML ESMIKKPRPT RAEGSDVANA VLDGADCIML 

       370        380        390        400        410        420 
SGETAKGDYP LEAVRMQHAI AREAEAAMFH RQQFEEILRH SVHHREPADA MAAGAVEASF 

       430        440        450        460        470        480 
KCLAAALIVM TESGRSAHLV SRYRPRAPII AVTRNDQTAR QAHLYRGVFP VLCKQPAHDA 

       490        500        510        520        530 
WAEDVDLRVN LGMNVGKARG FFKTGDLVIV LTGWRPGSGY TNTMRVVPVP 

« Hide

References

[1]"Primary structure of chicken muscle pyruvate kinase mRNA."
Lonberg N., Gilbert W.
Proc. Natl. Acad. Sci. U.S.A. 80:3661-3665(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Intron/exon structure of the chicken pyruvate kinase gene."
Lonberg N., Gilbert W.
Cell 40:81-90(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00903 mRNA. Translation: AAA49021.1.
M18793 expand/collapse EMBL AC list , M10619, M18788, M18789, M18790, M18791, M18792 Genomic DNA. Translation: AAA49020.1.
PIRKICHPM. I50408.
RefSeqNP_990800.1. NM_205469.1.
UniGeneGga.4299.

3D structure databases

ProteinModelPortalP00548.
SMRP00548. Positions 12-530.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676705. 2 interactions.
IntActP00548. 1 interaction.
STRING9031.ENSGALP00000034108.

Proteomic databases

PaxDbP00548.
PRIDEP00548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000003100; ENSGALP00000003096; ENSGALG00000001992.
GeneID396456.
KEGGgga:396456.

Organism-specific databases

CTD396456.

Phylogenomic databases

eggNOGCOG0469.
GeneTreeENSGT00390000008859.
HOGENOMHOG000021559.
HOVERGENHBG000941.
KOK00873.
PhylomeDBP00548.

Enzyme and pathway databases

ReactomeREACT_115655. Metabolism.
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.
IPR018209. Pyrv_Knase_AS.
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.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816497.
PROP00548.

Entry information

Entry nameKPYM_CHICK
AccessionPrimary (citable) accession number: P00548
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways