KPYK_DROME
ID KPYK_DROME Reviewed; 533 AA.
AC O62619; C3KGI0; Q86PE3; Q8MT14; Q9VD24;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=PyK; ORFNames=CG7070;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A).
RC STRAIN=Canton-S;
RA Chien Y.-C., Zhu Y.-J., Chuen C.-M.;
RT "Complementary DNA cloning and analysis of gene structure of pyruvate
RT kinase from Drosophila melanogaster.";
RL Zool. Stud. 38:322-332(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=3920304; DOI=10.1093/oxfordjournals.jhered.a110015;
RA Rust K.J., Collier G.E.;
RT "Localization of a dosage sensitive region for pyruvate kinase in
RT Drosophila melanogaster.";
RL J. Hered. 76:39-44(1985).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=O62619-1; Sequence=Displayed;
CC Name=B;
CC IsoId=O62619-2; Sequence=VSP_002885;
CC -!- TISSUE SPECIFICITY: In adults expressed predominantly in the thorax.
CC {ECO:0000269|PubMed:3920304}.
CC -!- DEVELOPMENTAL STAGE: Low levels in larvae and pupae, but increases in
CC young adults, becoming relatively stable in two-day-old flies.
CC {ECO:0000269|PubMed:3920304}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; AF062478; AAC16244.1; -; Genomic_DNA.
DR EMBL; AF061507; AAC15808.1; -; mRNA.
DR EMBL; AE014297; AAF55979.3; -; Genomic_DNA.
DR EMBL; AE014297; AAN14373.1; -; Genomic_DNA.
DR EMBL; AY118442; AAM48471.1; -; mRNA.
DR EMBL; BT003180; AAO24935.1; -; mRNA.
DR EMBL; BT082045; ACO95723.1; -; mRNA.
DR RefSeq; NP_524448.3; NM_079724.3. [O62619-1]
DR RefSeq; NP_732723.1; NM_170004.2. [O62619-2]
DR AlphaFoldDB; O62619; -.
DR SMR; O62619; -.
DR BioGRID; 67578; 31.
DR DIP; DIP-19290N; -.
DR IntAct; O62619; 23.
DR MINT; O62619; -.
DR STRING; 7227.FBpp0083611; -.
DR PaxDb; O62619; -.
DR PRIDE; O62619; -.
DR DNASU; 42620; -.
DR EnsemblMetazoa; FBtr0084213; FBpp0083610; FBgn0267385. [O62619-2]
DR EnsemblMetazoa; FBtr0084214; FBpp0083611; FBgn0267385. [O62619-1]
DR GeneID; 42620; -.
DR KEGG; dme:Dmel_CG7070; -.
DR CTD; 42620; -.
DR FlyBase; FBgn0267385; PyK.
DR VEuPathDB; VectorBase:FBgn0267385; -.
DR eggNOG; KOG2323; Eukaryota.
DR GeneTree; ENSGT00390000008859; -.
DR InParanoid; O62619; -.
DR PhylomeDB; O62619; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-70171; Glycolysis.
DR SignaLink; O62619; -.
DR UniPathway; UPA00109; UER00188.
DR BioGRID-ORCS; 42620; 1 hit in 3 CRISPR screens.
DR ChiTaRS; PyK; fly.
DR GenomeRNAi; 42620; -.
DR PRO; PR:O62619; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0267385; Expressed in thoracico-abdominal ganglion (Drosophila) and 28 other tissues.
DR Genevisible; O62619; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0043186; C:P granule; IPI:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; ISS:FlyBase.
DR GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
DR GO; GO:0006096; P:glycolytic process; ISS:FlyBase.
DR GO; GO:0006090; P:pyruvate metabolic process; ISS:FlyBase.
DR GO; GO:0009744; P:response to sucrose; IMP:FlyBase.
DR CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Potassium; Pyruvate; Reference proteome;
KW Transferase.
FT CHAIN 1..533
FT /note="Pyruvate kinase"
FT /id="PRO_0000112099"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 78..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 78
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 273
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_002885"
FT CONFLICT 180
FT /note="D -> N (in Ref. 1; AAC16244/AAC15808)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="I -> F (in Ref. 4; AAO24935)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="L -> F (in Ref. 1; AAC16244/AAC15808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 57440 MW; A8376B72F040EEDB CRC64;
MVNVTIYDEA PQLKPNEVPQ NMAAGADTQL EHMCRLQFDS PVPHVRLSGI VCTIGPASSS
VEMLEKMMAT GMNIARMNFS HGSHEYHAAT VANVRQAVKN YSAKLGYEHP VAIALDTKGP
EIRTGLIGGS GTAEIELKKG EKIKLTTNKE FLEKGSLEIV YVDYENIVNV VKPGNRVFVD
DGLISLIVRE VGKDSLTCEV ENGGSLGSRK GVNLPGVPVD LPAVSEKDKS DLLFGVEQEV
DMIFASFIRN AAALTEIRKV LGEKGKNIKI ISKIENQQGM HNLDEIIEAG DGIMVARGDL
GIEIPAEKVF LAQKAMIARC NKAGKPVICA TQMLESMVKK PRPTRAEISD VANAVLDGAD
CVMLSGETAK GEYPLECVLT MAKTCKEAEA ALWHQNLFND LVRGAGTIDA SHAAAIAAVE
AATKAKASAI VVITTSGKSA FQVSKYRPRC PIIAVTRFAQ TARQAHLYRG LVPLIYKEPG
LGDWLKDVDV RVQFGLQVGK KNGFIKTGDS VVVVTGWKQG SGFTNTIRIV TVE
