O62619 (KPYK_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	PyK
ORF Names:	CG7070

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	533 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium. Potassium.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer By similarity.
Tissue specificity	In adults expressed predominantly in the thorax. Ref.6
Developmental stage	Low levels in larvae and pupae, but increases in young adults, becoming relatively stable in two-day-old flies. Ref.6
Sequence similarities	Belongs to the pyruvate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Coding sequence diversity	Alternative splicing
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 Non-traceable author statement. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay PubMed 14668392. Source: FlyBase lipid particle Inferred from direct assay PubMed 16543254PubMed 16979555. Source: FlyBase
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 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: O62619-1)

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.

Isoform B (identifier: O62619-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 533	533	Pyruvate kinase		PRO_0000112099
Sites
	Metal binding	78	1	Potassium By similarity
	Metal binding	80	1	Potassium By similarity
	Metal binding	116	1	Potassium By similarity
	Metal binding	117	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	275	1	Magnesium By similarity
	Metal binding	299	1	Magnesium By similarity
	Binding site	76	1	Substrate By similarity
	Binding site	298	1	Substrate; via amide nitrogen By similarity
	Binding site	299	1	Substrate; via amide nitrogen By similarity
	Binding site	331	1	Substrate By similarity
	Site	273	1	Transition state stabilizer By similarity
Natural variations
	Alternative sequence	1 – 21	21	Missing in isoform B.		VSP_002885
Experimental info
	Sequence conflict	180	1	D → N in AAC16244. Ref.1
	Sequence conflict	180	1	D → N in AAC15808. Ref.1
	Sequence conflict	271	1	I → F in AAO24935. Ref.4
	Sequence conflict	397	1	L → F in AAC16244. Ref.1
	Sequence conflict	397	1	L → F in AAC15808. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified January 27, 2003. Version 2. Checksum: A8376B72F040EEDB	FASTA	533	57,440
	10 20 30 40 50 60 MVNVTIYDEA PQLKPNEVPQ NMAAGADTQL EHMCRLQFDS PVPHVRLSGI VCTIGPASSS 70 80 90 100 110 120 VEMLEKMMAT GMNIARMNFS HGSHEYHAAT VANVRQAVKN YSAKLGYEHP VAIALDTKGP 130 140 150 160 170 180 EIRTGLIGGS GTAEIELKKG EKIKLTTNKE FLEKGSLEIV YVDYENIVNV VKPGNRVFVD 190 200 210 220 230 240 DGLISLIVRE VGKDSLTCEV ENGGSLGSRK GVNLPGVPVD LPAVSEKDKS DLLFGVEQEV 250 260 270 280 290 300 DMIFASFIRN AAALTEIRKV LGEKGKNIKI ISKIENQQGM HNLDEIIEAG DGIMVARGDL 310 320 330 340 350 360 GIEIPAEKVF LAQKAMIARC NKAGKPVICA TQMLESMVKK PRPTRAEISD VANAVLDGAD 370 380 390 400 410 420 CVMLSGETAK GEYPLECVLT MAKTCKEAEA ALWHQNLFND LVRGAGTIDA SHAAAIAAVE 430 440 450 460 470 480 AATKAKASAI VVITTSGKSA FQVSKYRPRC PIIAVTRFAQ TARQAHLYRG LVPLIYKEPG 490 500 510 520 530 LGDWLKDVDV RVQFGLQVGK KNGFIKTGDS VVVVTGWKQG SGFTNTIRIV TVE
	Isoform B [UniParc]. Checksum: 4ED4A31F0686874B	FASTA	512	55,059
	10 20 30 40 50 60 MAAGADTQLE HMCRLQFDSP VPHVRLSGIV CTIGPASSSV EMLEKMMATG MNIARMNFSH 70 80 90 100 110 120 GSHEYHAATV ANVRQAVKNY SAKLGYEHPV AIALDTKGPE IRTGLIGGSG TAEIELKKGE 130 140 150 160 170 180 KIKLTTNKEF LEKGSLEIVY VDYENIVNVV KPGNRVFVDD GLISLIVREV GKDSLTCEVE 190 200 210 220 230 240 NGGSLGSRKG VNLPGVPVDL PAVSEKDKSD LLFGVEQEVD MIFASFIRNA AALTEIRKVL 250 260 270 280 290 300 GEKGKNIKII SKIENQQGMH NLDEIIEAGD GIMVARGDLG IEIPAEKVFL AQKAMIARCN 310 320 330 340 350 360 KAGKPVICAT QMLESMVKKP RPTRAEISDV ANAVLDGADC VMLSGETAKG EYPLECVLTM 370 380 390 400 410 420 AKTCKEAEAA LWHQNLFNDL VRGAGTIDAS HAAAIAAVEA ATKAKASAIV VITTSGKSAF 430 440 450 460 470 480 QVSKYRPRCP IIAVTRFAQT ARQAHLYRGL VPLIYKEPGL GDWLKDVDVR VQFGLQVGKK 490 500 510 NGFIKTGDSV VVVTGWKQGS GFTNTIRIVT VE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complementary DNA cloning and analysis of gene structure of pyruvate kinase from Drosophila melanogaster." Chien Y.-C., Zhu Y.-J., Chuen C.-M. Zool. Stud. 38:322-332(1999) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A). Strain: Canton-S.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B). Strain: Berkeley. Tissue: Embryo and Head.
[5]	Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). Strain: Berkeley.
[6]	"Localization of a dosage sensitive region for pyruvate kinase in Drosophila melanogaster." Rust K.J., Collier G.E. J. Hered. 76:39-44(1985) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF062478 Genomic DNA. Translation: AAC16244.1. AF061507 mRNA. Translation: AAC15808.1. AE014297 Genomic DNA. Translation: AAF55979.3. AE014297 Genomic DNA. Translation: AAN14373.1. AY118442 mRNA. Translation: AAM48471.1. BT003180 mRNA. Translation: AAO24935.1. BT082045 mRNA. Translation: ACO95723.1.
RefSeq	NP_524448.3. NM_079724.2. NP_732723.1. NM_170004.1.
UniGene	Dm.7108.
3D structure databases
ProteinModelPortal	O62619.
SMR	O62619. Positions 20-532.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-19290N.
IntAct	O62619. 2 interactions.
Proteomic databases
PaxDb	O62619.
PRIDE	O62619.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0084214; FBpp0083611; FBgn0003178.
GeneID	42620.
KEGG	dme:Dmel_CG7070.
Organism-specific databases
CTD	42620.
FlyBase	FBgn0003178. PyK.
Phylogenomic databases
eggNOG	COG0469.
GeneTree	ENSGT00390000008859.
InParanoid	O62619.
KO	K00873.
OMA	VFGIEQG.
OrthoDB	EOG41ZCS3.
PhylomeDB	O62619.
Enzyme and pathway databases
UniPathway	UPA00109; UER00188.
Gene expression databases
Bgee	O62619.
GermOnline	CG7070. Drosophila melanogaster.
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-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]
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...
Other
GenomeRNAi	42620.
NextBio	829729.

Entry information

Entry name

KPYK_DROME

Accession

Primary (citable) accession number: O62619
Secondary accession number(s): C3KGI0 , Q86PE3, Q8MT14, Q9VD24

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 27, 2003
Last modified:	May 29, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project