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Protein

Pyruvate kinase 1

Gene

PYK1

Organism
Trypanosoma brucei brucei
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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-RKP30615.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase 1 (EC:2.7.1.40)
Short name:
PK 1
Gene namesi
Name:PYK1
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001121031 – 499Pyruvate kinase 1Add BLAST499

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

Secondary structure

1499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 8Combined sources6
Beta strandi12 – 14Combined sources3
Beta strandi22 – 27Combined sources6
Turni30 – 32Combined sources3
Helixi35 – 44Combined sources10
Beta strandi46 – 52Combined sources7
Helixi58 – 75Combined sources18
Beta strandi80 – 84Combined sources5
Beta strandi90 – 92Combined sources3
Helixi96 – 98Combined sources3
Beta strandi99 – 102Combined sources4
Beta strandi107 – 111Combined sources5
Helixi114 – 116Combined sources3
Beta strandi122 – 128Combined sources7
Helixi132 – 135Combined sources4
Beta strandi141 – 144Combined sources4
Turni145 – 148Combined sources4
Beta strandi149 – 158Combined sources10
Beta strandi161 – 166Combined sources6
Beta strandi170 – 173Combined sources4
Beta strandi177 – 179Combined sources3
Helixi192 – 204Combined sources13
Beta strandi207 – 211Combined sources5
Helixi217 – 227Combined sources11
Turni228 – 233Combined sources6
Beta strandi234 – 240Combined sources7
Helixi243 – 247Combined sources5
Helixi249 – 255Combined sources7
Beta strandi256 – 262Combined sources7
Helixi263 – 269Combined sources7
Helixi272 – 274Combined sources3
Helixi275 – 289Combined sources15
Beta strandi293 – 298Combined sources6
Helixi301 – 304Combined sources4
Beta strandi306 – 308Combined sources3
Helixi311 – 323Combined sources13
Beta strandi326 – 331Combined sources6
Helixi332 – 335Combined sources4
Helixi340 – 356Combined sources17
Helixi362 – 369Combined sources8
Helixi377 – 392Combined sources16
Beta strandi395 – 400Combined sources6
Beta strandi402 – 404Combined sources3
Helixi405 – 412Combined sources8
Beta strandi419 – 424Combined sources6
Helixi426 – 431Combined sources6
Helixi432 – 434Combined sources3
Beta strandi438 – 442Combined sources5
Helixi445 – 448Combined sources4
Helixi455 – 467Combined sources13
Beta strandi476 – 481Combined sources6
Beta strandi492 – 497Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HYVX-ray2.30A/B1-499[»]
4HYWX-ray2.35A/B1-499[»]
4KCTX-ray1.95A/B1-499[»]
4KCUX-ray2.35A/B1-499[»]
4KCVX-ray2.18A/B1-499[»]
4KCWX-ray2.50A/B1-499[»]
ProteinModelPortaliP30615.
SMRiP30615.
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.

P30615-1 [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
SFAPGDIVCV TTDPAYEKVG TKEKFYIDYP QLTNAVRPGG SIYVDDGVMT
160 170 180 190 200
LRVVSKEDDR 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):54,467
Last modified:April 1, 1993 - v1
Checksum:i1D40AD5352B272C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57950 Genomic DNA. Translation: CAA41018.1.
PIRiS17648.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57950 Genomic DNA. Translation: CAA41018.1.
PIRiS17648.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HYVX-ray2.30A/B1-499[»]
4HYWX-ray2.35A/B1-499[»]
4KCTX-ray1.95A/B1-499[»]
4KCUX-ray2.35A/B1-499[»]
4KCVX-ray2.18A/B1-499[»]
4KCWX-ray2.50A/B1-499[»]
ProteinModelPortaliP30615.
SMRiP30615.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
SABIO-RKP30615.

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 nameiKPYK1_TRYBB
AccessioniPrimary (citable) accession number: P30615
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 2, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme

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

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.