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Protein

Pyruvate kinase 2

Gene

PYK2

Organism
Trypanosoma brucei brucei
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Activated by fructose 2,6-bisphosphate, activated by the effector in a cooperative manner.

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, cytosolic, Glyceraldehyde-3-phosphate dehydrogenase, glycosomal
  2. Phosphoglycerate kinase, cytosolic, Phosphoglycerate kinase A, Phosphoglycerate kinase A, Phosphoglycerate kinase, glycosomal, Phosphoglycerate kinase, cytosolic
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. Pyruvate kinase 1 (PYK1), Pyruvate kinase 2 (PYK2)
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 sitei50SubstrateBy similarity1
Metal bindingi52PotassiumBy similarity1
Metal bindingi54PotassiumBy similarity1
Metal bindingi84PotassiumBy similarity1
Metal bindingi85Potassium; via carbonyl oxygenBy similarity1
Sitei239Transition state stabilizerBy similarity1
Metal bindingi241MagnesiumSequence analysis1
Binding sitei264Substrate; via amide nitrogenBy similarity1
Metal bindingi265MagnesiumBy similarity1
Binding sitei265Substrate; via amide nitrogenBy similarity1
Binding sitei297SubstrateBy 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

SABIO-RKP30616.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase 2 (EC:2.7.1.40)
Short name:
PK 2
Gene namesi
Name:PYK2
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001121041 – 499Pyruvate kinase 2Add BLAST499

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP30616.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

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]

Sequencei

Sequence statusi: Complete.

P30616-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQLEHNIGL SIFEPVAKHR ANRIVCTIGP STQSVEALKN LMKSGMSVAR
60 70 80 90 100
MNFSHGSHEY HQTTINNVRA AAAELGLHIG IALDTKGPEI RTGLFKDGEV
110 120 130 140 150
TFAPGDIVCV TTDPAYEKVG TKEKFYIDYP QLTKAVPVGG SIYVDDGVMT
160 170 180 190 200
LRVLSKEDDR TLKCHVNNHH RLTDRRGINL PGCEVDLPAV SEKDRKDLEF
210 220 230 240 250
GVAQGVDMIF ASFIRTAEQV REVRAALGEK GKDILIISKI ENHQGVQNID
260 270 280 290 300
SIIEASNGIM VARGDLGVEI PAEKVCVAQM CIISKCNVVG KPVICATQML
310 320 330 340 350
ESMTSNPRPT RAEVSDVANA VLNGADCVML SGETAKGKYP NEVVQYMARI
360 370 380 390 400
CVEAQSATHD TVMFNSIKNL QKIPMCPEEA VCSSAVASAF EVQAKAMLVL
410 420 430 440 450
SNTGRSARLI SKYRPNCPII CVTTRLQTCR QLNVTRSVVS VFYDAAKSGE
460 470 480 490
DKDKEKRVKL GLDFAKKEKY ASTGDVVVVV HADHSVKGYP NQTRLIYLP
Length:499
Mass (Da):54,452
Last modified:April 1, 1993 - v1
Checksum:i7FE8238E73E45CA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57951 Genomic DNA. Translation: CAA41019.1.
PIRiS17649.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57951 Genomic DNA. Translation: CAA41019.1.
PIRiS17649.

3D structure databases

ProteinModelPortaliP30616.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
SABIO-RKP30616.

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 nameiKPYK2_TRYBB
AccessioniPrimary (citable) accession number: P30616
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 5, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

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.