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Protein

Pyruvate kinase PKLR

Gene

PKLR

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a key role in glycolysis.By similarity

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity
  • K+By similarity

Enzyme regulationi

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

Pathwayi: glycolysis

This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (LOC106559694), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (LOC100683724), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (LOC106558132), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (LOC106558049), Glyceraldehyde-3-phosphate dehydrogenase (GAPDHS), Glyceraldehyde-3-phosphate dehydrogenase (LOC477441)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase PKLR (PKLR), Pyruvate kinase (PKLR), Pyruvate kinase (PKLR), Pyruvate kinase (pklr)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei116SubstrateBy similarity1
Metal bindingi118PotassiumBy similarity1
Metal bindingi120PotassiumBy similarity1
Metal bindingi156PotassiumBy similarity1
Metal bindingi157Potassium; via carbonyl oxygenBy similarity1
Sitei313Transition state stabilizerBy similarity1
Metal bindingi315MagnesiumBy similarity1
Binding sitei338Substrate; via amide nitrogenBy similarity1
Metal bindingi339MagnesiumBy similarity1
Binding sitei339Substrate; via amide nitrogenBy similarity1
Binding sitei371SubstrateBy similarity1
Binding sitei525Allosteric activatorBy similarity1
Binding sitei532Allosteric activatorBy similarity1

GO - Molecular functioni

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 PKLR (EC:2.7.1.40)
Alternative name(s):
Pyruvate kinase isozymes L/R
Gene namesi
Name:PKLR
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componentsi: Unassembled WGS sequence, Unplaced

Pathology & Biotechi

Involvement in diseasei

Defects in PKLR are a cause of inherited hemolytic anemia, an autosomal recessive disease of the Basenji dog that closely resembles human pyruvate kinase deficiency.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001120931 – 574Pyruvate kinase PKLRAdd BLAST574

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2PhosphoserineBy similarity1
Modified residuei19PhosphoserineBy similarity1
Modified residuei26PhosphoserineBy similarity1
Modified residuei43PhosphoserineBy similarity1
Modified residuei105N6-acetyllysineBy similarity1
Modified residuei109N6-succinyllysineBy similarity1
Modified residuei140PhosphoserineBy similarity1
Modified residuei148PhosphotyrosineBy similarity1
Modified residuei209N6-acetyllysine; alternateBy similarity1
Modified residuei209N6-succinyllysine; alternateBy similarity1
Modified residuei292PhosphoserineBy similarity1
Modified residuei313N6-acetyllysineBy similarity1
Modified residuei365N6-acetyllysine; alternateBy similarity1
Modified residuei365N6-succinyllysine; alternateBy similarity1
Modified residuei541N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ29536.
PRIDEiQ29536.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000024956.

Structurei

3D structure databases

ProteinModelPortaliQ29536.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni475 – 480Allosteric activator bindingBy similarity6
Regioni559 – 564Allosteric activator bindingBy similarity6

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiKOG2323. Eukaryota.
COG0469. LUCA.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiQ29536.
KOiK12406.

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.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform R-type (identifier: Q29536-1) [UniParc]FASTAAdd to basket
Also known as: PKR

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

        10         20         30         40         50
MSSQENIQPQ ELWSRISKSQ RDLAKSILIG APGGPAGYLR RASVAQLTLE
60 70 80 90 100
LGTAFFQQQQ LSAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASHS
110 120 130 140 150
VERLKEMIKA GMNIARLNFS HGSHEYHAQS IANIREAVES FATSPLGYRP
160 170 180 190 200
VAIALDTKGP EIRTGVLKGG PETEVELVKG SWVLVTVDPA FRTLGDAHTV
210 220 230 240 250
WVDYPNIVKV VPVGGRIFID DGLISLQVKK IDRKGLETQV ENGGLLGSRK
260 270 280 290 300
GVNLPGAEVD LPGLSEQDAQ DLRFGVEHNV DIVFASFVRK ASDVAAIRAA
310 320 330 340 350
LGPEGRTIKI ISKIENHEGV KKFDEILEVS DGIMVARGDL GIEIPAEKVF
360 370 380 390 400
LAQKMMIGRC NLAGKPVVCA TQMLESMITK PRPTRAETSD VANAVLDGAD
410 420 430 440 450
CIMLSGETAK GKFPVEAVKM QHAIAREAEA AVYHRQLFEE LRRAAPLSRD
460 470 480 490 500
PTEVTAIGAV EAAFKCCAAA IIVLTKTGRS AQLLSRYRPR AAVIAVTRSA
510 520 530 540 550
QAARQAHLCR GVFPLLYSEP PEAIWADDVD RRVQFGIESG KLRGFLRVGD
560 570
LVIVVTGWRP GSGYTNIMRV LSIS
Length:574
Mass (Da):62,048
Last modified:March 21, 2012 - v2
Checksum:iF18E28450B1C7F30
GO
Isoform L-type (identifier: Q29536-2) [UniParc]FASTAAdd to basket
Also known as: PKL

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MSSQENIQPQELWSRISKSQRDLAKSILIGAPG → ME

Show »
Length:543
Mass (Da):58,657
Checksum:iC4976F7282F91798
GO

Sequence cautioni

The sequence DN338485 differs from that shown. Derived from EST data.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti423A → R in AAB31627 (PubMed:7520391).Curated1
Sequence conflicti458 – 459GA → AT in AAB31627 (PubMed:7520391).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0424441 – 33MSSQE…IGAPG → ME in isoform L-type. 1 PublicationAdd BLAST33

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03005338 Genomic DNA. No translation available.
AH004600 mRNA. Translation: AAB31627.2.
DN338485 mRNA. No translation available.
RefSeqiNP_001242947.1. NM_001256018.1.
NP_001243191.1. NM_001256262.1. [Q29536-1]
UniGeneiCfa.8012.

Genome annotation databases

GeneIDi490425.
KEGGicfa:490425.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03005338 Genomic DNA. No translation available.
AH004600 mRNA. Translation: AAB31627.2.
DN338485 mRNA. No translation available.
RefSeqiNP_001242947.1. NM_001256018.1.
NP_001243191.1. NM_001256262.1. [Q29536-1]
UniGeneiCfa.8012.

3D structure databases

ProteinModelPortaliQ29536.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000024956.

Proteomic databases

PaxDbiQ29536.
PRIDEiQ29536.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi490425.
KEGGicfa:490425.

Organism-specific databases

CTDi5313.

Phylogenomic databases

eggNOGiKOG2323. Eukaryota.
COG0469. LUCA.
HOGENOMiHOG000021559.
HOVERGENiHBG000941.
InParanoidiQ29536.
KOiK12406.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiKPYR_CANLF
AccessioniPrimary (citable) accession number: Q29536
Secondary accession number(s): F1P923, F1PXP8, F1PY57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 21, 2012
Last modified: July 6, 2016
This is version 116 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 and M2. 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.

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.