Pyruvate kinase 1 - Trypanosoma brucei brucei

Preferred order of sections

Names and origin

Protein names

Recommended name:
Pyruvate kinase 1
Short name=PK 1
EC=2.7.1.40

Gene names

Name:

PYK1

Organism

Trypanosoma brucei brucei

Taxonomic identifier

5702 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma ›

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium. Potassium.
Enzyme regulation	Activated by fructose 2,6-bisphosphate, activated by the effector in a cooperative manner.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the pyruvate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro potassium ion binding Inferred from electronic annotation. Source: InterPro pyruvate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 499

499

Pyruvate kinase 1

PRO_0000112103

Sites

Metal binding

52

1

Potassium By similarity

Metal binding

54

1

Potassium By similarity

Metal binding

84

1

Potassium By similarity

Metal binding

85

1

Potassium; via carbonyl oxygen By similarity

Metal binding

241

1

Magnesium Potential

Metal binding

265

1

Magnesium By similarity

Binding site

50

1

Substrate By similarity

Binding site

264

1

Substrate; via amide nitrogen By similarity

Binding site

265

1

Substrate; via amide nitrogen By similarity

Binding site

297

1

Substrate By similarity

Site

239

1

Transition state stabilizer By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P30615 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 1D40AD5352B272C6
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FASTA

499

54,467

        10         20         30         40         50         60 
MSQLEHNIGL SIFEPVAKHR ANRIVCTIGP STQSVEALKN LMKSGMSVAR MNFSHGSHEY 

        70         80         90        100        110        120 
HQTTINNVRA AAAELGLHIG IALDTKGPEI RTGLFKDGEV SFAPGDIVCV TTDPAYEKVG 

       130        140        150        160        170        180 
TKEKFYIDYP QLTNAVRPGG SIYVDDGVMT LRVVSKEDDR TLKCHVNNHH RLTDRRGINL 

       190        200        210        220        230        240 
PGCEVDLPAV SEKDRKDLEF GVAQGVDMIF ASFIRTAEQV REVRAALGEK GKDILIISKI 

       250        260        270        280        290        300 
ENHQGVQNID SIIEASNGIM VARGDLGVEI PAEKVCVAQM CIISKCNVVG KPVICATQML 

       310        320        330        340        350        360 
ESMTSNPRPT RAEVSDVANA VLNGADCVML SGETAKGKYP NEVVQYMARI CVEAQSATHD 

       370        380        390        400        410        420 
TVMFNSIKNL QKIPMCPEEA VCSSAVASAF EVQAKAMLVL SNTGRSARLI SKYRPNCPII 

       430        440        450        460        470        480 
CVTTRLQTCR QLNVTRSVVS VFYDAAKSGE DKDKEKRVKL GLDFAKKEKY ASTGDVVVVV 

       490 
HADHSVKGYP NQTRLIYLP

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References

[1]

"Molecular cloning and analysis of two tandemly linked genes for pyruvate kinase of Trypanosoma brucei."
Allert S., Ernest I., Poliszczak A., Opperdoes F.R., Michels P.A.M.
Eur. J. Biochem. 200:19-27(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 427.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X57950 Genomic DNA. Translation: CAA41018.1.
PIR	S17648.
3D structure databases
ProteinModelPortal	P30615.
SMR	P30615. Positions 2-496.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
SABIO-RK	P30615.
UniPathway	UPA00109; UER00188.
Family and domain databases
Gene3D	2.40.33.10. 1 hit. 3.20.20.60. 2 hits. 3.40.1380.20. 1 hit.
InterPro	IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase. 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]
PANTHER	PTHR11817. PTHR11817. 1 hit.
Pfam	PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
SUPFAM	SSF50800. PK_B_barrel_like. 1 hit. SSF52935. Pyruvate_kinase. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01064. pyruv_kin. 1 hit.
PROSITE	PS00110. PYRUVATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPYK1_TRYBB

Accession

Primary (citable) accession number: P30615

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents