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   24-JAN-2024, entry version 187.
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; 32.
DR   DIP; DIP-19290N; -.
DR   IntAct; O62619; 23.
DR   MINT; O62619; -.
DR   STRING; 7227.FBpp0083611; -.
DR   GlyGen; O62619; 1 site, 1 O-linked glycan (1 site).
DR   PaxDb; 7227-FBpp0083611; -.
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   AGR; FB:FBgn0267385; -.
DR   CTD; 42620; -.
DR   FlyBase; FBgn0267385; PyK.
DR   VEuPathDB; VectorBase:FBgn0267385; -.
DR   eggNOG; KOG2323; Eukaryota.
DR   GeneTree; ENSGT00390000008859; -.
DR   InParanoid; O62619; -.
DR   OMA; RVHHIGE; -.
DR   OrthoDB; 312683at2759; -.
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 cell types or tissues.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR   Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 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   NCBIfam; TIGR01064; pyruv_kin; 1.
DR   PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
DR   Genevisible; O62619; DM.
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
//