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P11979

- KPYM_FELCA

UniProt

P11979 - KPYM_FELCA

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Protein

Pyruvate kinase PKM

Gene
PKM, PKM2
Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation By similarity.

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Magnesium.
Potassium.

Enzyme regulationi

Allosterically activated by D-fructose 1,6-bisphosphate (FBP). Inhibited by oxalate and 3,3',5-triiodo-L-thyronine (T3). The activity of the tetrameric form is inhibited by PML. Selective binding to tyrosine-phosphorylated peptides releases the allosteric activator FBP, leading to inhibition of PKM enzymatic activity, this diverts glucose metabolites from energy production to anabolic processes when cells are stimulated by certain growth factors. Glycolytic flux are highly dependent on de novo biosynthesis of serine and glycine, and serine is a natural ligand and allosteric activator By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701Serine By similarity
Binding sitei73 – 731Substrate By similarity
Metal bindingi75 – 751Potassium By similarity
Metal bindingi77 – 771Potassium By similarity
Binding sitei106 – 1061Serine By similarity
Metal bindingi113 – 1131Potassium By similarity
Metal bindingi114 – 1141Potassium; via carbonyl oxygen By similarity
Sitei270 – 2701Transition state stabilizer By similarity
Metal bindingi272 – 2721Magnesium By similarity
Binding sitei295 – 2951Substrate; via amide nitrogen By similarity
Metal bindingi296 – 2961Magnesium By similarity
Binding sitei296 – 2961Substrate; via amide nitrogen By similarity
Binding sitei328 – 3281Substrate By similarity
Binding sitei464 – 4641Serine By similarity
Binding sitei482 – 4821D-fructose 1,6-bisphosphate; part of allosteric site By similarity
Binding sitei489 – 4891D-fructose 1,6-bisphosphate; part of allosteric site By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
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

UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase PKM (EC:2.7.1.40)
Alternative name(s):
Pyruvate kinase muscle isozyme
Gene namesi
Name:PKM
Synonyms:PKM2
OrganismiFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifieri9685 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
ProteomesiUP000011712: Unplaced

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 531530Pyruvate kinase PKMPRO_0000112087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei37 – 371Phosphoserine By similarity
Modified residuei62 – 621N6-acetyllysine By similarity
Modified residuei66 – 661N6-succinyllysine By similarity
Modified residuei89 – 891N6-acetyllysine By similarity
Modified residuei105 – 1051Phosphotyrosine By similarity
Modified residuei148 – 1481Phosphotyrosine By similarity
Modified residuei166 – 1661N6-acetyllysine; alternate By similarity
Modified residuei166 – 1661N6-succinyllysine; alternate By similarity
Modified residuei175 – 1751Phosphotyrosine By similarity
Modified residuei195 – 1951Phosphothreonine By similarity
Modified residuei266 – 2661N6-acetyllysine By similarity
Modified residuei270 – 2701N6-acetyllysine By similarity
Modified residuei305 – 3051N6-acetyllysine By similarity
Modified residuei322 – 3221N6-acetyllysine; alternate By similarity
Modified residuei322 – 3221N6-succinyllysine; alternate By similarity
Modified residuei475 – 4751N6-acetyllysine By similarity
Modified residuei498 – 4981N6-succinyllysine By similarity

Post-translational modificationi

ISGylated By similarity.
Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy By similarity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP11979.

Interactioni

Subunit structurei

Monomer and homotetramer. Exists as a monomer in the absence of FBP, and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds T3. Tetramer formation induces pyruvate kinase activity. Interacts with HERC1 POU5F1 and PML By similarity.

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000000606.

Structurei

Secondary structure

1
531
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 214
Helixi26 – 316
Beta strandi45 – 506
Turni53 – 553
Helixi58 – 669
Beta strandi69 – 757
Helixi81 – 9616
Turni97 – 1004
Turni102 – 1043
Beta strandi109 – 1135
Beta strandi119 – 1213
Beta strandi139 – 1435
Beta strandi148 – 1514
Beta strandi154 – 1607
Helixi164 – 1674
Beta strandi173 – 1764
Turni177 – 1804
Beta strandi181 – 1888
Beta strandi190 – 19910
Beta strandi208 – 2103
Helixi223 – 23412
Beta strandi238 – 2436
Helixi248 – 25811
Turni259 – 2646
Beta strandi265 – 2717
Helixi275 – 2784
Helixi280 – 2867
Beta strandi287 – 2937
Helixi294 – 3007
Turni303 – 3053
Helixi306 – 32015
Beta strandi324 – 3318
Helixi332 – 3354
Helixi342 – 35413
Beta strandi357 – 3626
Helixi363 – 3664
Helixi371 – 38717
Helixi391 – 40212
Helixi408 – 42316
Beta strandi428 – 4314
Beta strandi433 – 4353
Helixi436 – 4438
Beta strandi450 – 4556
Helixi457 – 4626
Helixi463 – 4653
Beta strandi469 – 4735
Helixi482 – 49918
Beta strandi508 – 5136
Beta strandi524 – 5296

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PKMX-ray2.60A2-531[»]
ProteinModelPortaliP11979.
SMRiP11979. Positions 13-531.

Miscellaneous databases

EvolutionaryTraceiP11979.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni307 – 531225Interaction with POU5F1 By similarityAdd
BLAST
Regioni432 – 4376D-fructose 1,6-bisphosphate binding; part of allosteric site By similarity
Regioni514 – 5218D-fructose 1,6-bisphosphate binding; part of allosteric site By similarity

Sequence similaritiesi

Belongs to the pyruvate kinase family.

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
OrthoDBiEOG78M01Q.
TreeFamiTF300390.

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.
IPR018209. Pyrv_Knase_AS.
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.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform M1 (identifier: P11979-1) [UniParc]FASTAAdd to Basket

Also known as: PKM1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSKPHSDVGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT    50
IGPASRSVEI LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRAATESFAS 100
DPIRYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME 150
KCDENVLWLD YKNICKVVEV GSKVYVDDGL ISLLVKEKGA DFLVTEVENG 200
GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD 250
VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE 300
IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN 350
AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAMF HRKLFEELVR 400
GSSHSTDLME AMAMGSVEAS YKCLAAALIV LTESGRSAHQ VARYRPRAPI 450
IAVTRNHQTA RQAHLYRGIF PVVCKDPVQE AWAEDVDLRV NLAMNVGKAR 500
GFFKHGDVVI VLTGWRPGSG FTNTMRVVPV P 531
Length:531
Mass (Da):58,046
Last modified:January 23, 2007 - v2
Checksum:i302475E32D6109A8
GO
Isoform M2 (identifier: P11979-2)

Also known as: PKM2

Sequence is not available
Length:
Mass (Da):

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091V → A AA sequence 1 Publication
Sequence conflicti226 – 2272IQ → FE AA sequence 1 Publication
Sequence conflicti232 – 2321G → Q AA sequence 1 Publication
Sequence conflicti235 – 2351Q → R AA sequence 1 Publication

Sequence databases

PIRiA25091.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

PIRi A25091.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PKM X-ray 2.60 A 2-531 [» ]
ProteinModelPortali P11979.
SMRi P11979. Positions 13-531.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9685.ENSFCAP00000000606.

Proteomic databases

PRIDEi P11979.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0469.
HOGENOMi HOG000021559.
HOVERGENi HBG000941.
OrthoDBi EOG78M01Q.
TreeFami TF300390.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .

Miscellaneous databases

EvolutionaryTracei P11979.

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProi IPR001697. 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 ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The structure of cat muscle pyruvate kinase."
    Muirhead H., Clayden D.A., Barford D., Lorimer C.G., Fothergill-Gilmore L.A., Schiltz E., Schmitt W.
    EMBO J. 5:475-481(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-531, ACETYLATION AT SER-2.
  2. "Hydroxylamine cleavage of cat skeletal-muscle pyruvate kinase: separation of the fragments and N-terminal sequence analysis."
    McAleese S.M., Hoar C.G., Dunbar B., Fothergill-Gilmore L.A.
    Biochem. Soc. Trans. 10:444-445(1982)
    Cited for: PROTEIN SEQUENCE OF 200-236.
  3. "A comparison of the structure and activity of cat and trout muscle pyruvate kinases."
    Harkins R.N., Nocton J.C., Russell M.P., Fothergill-Gilmore L.A., Muirhead H.
    Eur. J. Biochem. 136:341-346(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 314-330.
  4. "Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A."
    Stuart D.I., Levine M., Muirhead H., Stammers D.K.
    J. Mol. Biol. 134:109-142(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  5. "Three-dimensional structure of cat muscle pyruvate kinase at 3.1-A resolution."
    Stammers D.K., Muirhead H.
    J. Mol. Biol. 112:309-316(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
  6. "Three-dimensional structure of cat muscle pyruvate kinase at 6-A resolution."
    Stammers D.K., Muirhead H.
    J. Mol. Biol. 95:213-225(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
  7. "Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 A."
    Allen S.C., Muirhead H.
    Acta Crystallogr. D 52:499-504(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiKPYM_FELCA
AccessioniPrimary (citable) accession number: P11979
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 4 isozymes of pyruvate kinase in mammals (L, R, M1, M2) encoded by 2 different genes: PKLR and PKM. The L and R isozymes are generated from the PKLR by differential splicing of RNA; the M1 and M2 forms are produced from the PKM gene by differential splicing. L type is major isozyme in the liver, R is found in red cells, M1 is the main form in muscle, heart and brain, and M2 is found in early fetal tissues as well as in most cancer cells.

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, 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

External Data

Dasty 3

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