Q8SQP0 (KPYK_ENCCU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	PYK1
Ordered Locus Names:	ECU09_0640

Organism

Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) [Reference proteome]

Taxonomic identifier

284813 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Microsporidia › Apansporoblastina › Unikaryonidae › Encephalitozoon › Encephalitozoon cuniculi

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium By similarity. Potassium By similarity.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer By similarity.
Developmental stage	Expressed in late sporogonial stages.
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	Complete proteome Reference proteome
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 – 519	519	Pyruvate kinase		PRO_0000379473
Sites
	Metal binding	127	1	Potassium By similarity
	Metal binding	129	1	Potassium By similarity
	Metal binding	159	1	Potassium By similarity
	Metal binding	160	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	305	1	Magnesium Potential
	Metal binding	329	1	Magnesium By similarity
	Binding site	125	1	Substrate By similarity
	Binding site	328	1	Substrate; via amide nitrogen By similarity
	Binding site	329	1	Substrate; via amide nitrogen By similarity
	Binding site	361	1	Substrate By similarity
	Site	303	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8SQP0 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 6FEF3BF2FCA9DACD	FASTA	519	57,969
	10 20 30 40 50 60 MWLVEEKYLV PFYEYHYDML CRPYQCTCCQ ILGGWDFVIQ RPHHNGYSLH AARGCMLDYI 70 80 90 100 110 120 YSFGQDYVSY LQSTYHWSQK LDKFGKCLAQ AMRMVLTKIV CTIGPRTSSR EKIKELIDAG 130 140 150 160 170 180 MSIARLNFSH GSREAHLEVI RNIRDSRSGA GRHVSIALDT RGPEVRLRTP EMKDIKVEGG 190 200 210 220 230 240 EVLRFSLLSS EKDIWIPGVD LKSLGVDNRV FIDDGAIELR VVNVEEDGFE CEVLNSGMIK 250 260 270 280 290 300 SNKSMNFPGT DIGDRALGDE DKNDIAFGLE NGIDMVFASF VSCRADVEEI RRLVGSKVPV 310 320 330 340 350 360 VSKIESCLGM RNLKEIALCS DGVMIARGDL GVEIGLENMF SAQKRILYEV KREGRPVICA 370 380 390 400 410 420 TQMMESMTLK NAPNRSEISD VGNAVLDGCD CVMLSAESAV GMFPVETVKF MRSICADAER 430 440 450 460 470 480 YDMESRKGAG ACGVSSYVDG VVICSGTESQ IEKIYLSKPE TPIIVISESL WILRRFSIYR 490 500 510 GIIPVYGKGS EDAEATLRRL GLRGRFLAVG REDVRMVSV

References

[1]

"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi." Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P. Nature 414:450-453(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GB-M1.

[2]

"Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi (microsporidia): a reference map for proteins expressed in late sporogonial stages." Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C. Proteomics 6:3625-3635(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL STAGE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL590451 Genomic DNA. Translation: CAD27037.1.
RefSeq	XP_955618.1. XM_950525.1.
3D structure databases
HSSP	HSSP built from PDB template 1LIU based on UniProtKB P30613.
ProteinModelPortal	Q8SQP0.
ModBase	Search...
Protein-protein interaction databases
STRING	6035.ECU09_0640.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	860403.
KEGG	ecu:ECU09_0640.
Phylogenomic databases
eggNOG	COG0469.
HOGENOM	HOG000021559.
KO	K00873.
OMA	ESANGHY.
Enzyme and pathway databases
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. 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. [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.
ProtoNet	Search...

Entry information

Entry name

KPYK_ENCCU

Accession

Primary (citable) accession number: Q8SQP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 7, 2009
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program