ID KPYK_DICDI Reviewed; 507 AA. AC Q54RF5; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 24-JAN-2024, entry version 112. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; ORFNames=DDB_G0283247; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). RN [2] RP PROTEIN SEQUENCE OF 10-21; 78-91; 265-275 AND 476-489, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RA Bienvenut W.V., Veltman D.M., Insall R.H.; RL Submitted (JAN-2010) to UniProtKB. 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; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAFI02000051; EAL65862.1; -; Genomic_DNA. DR RefSeq; XP_639190.1; XM_634098.1. DR AlphaFoldDB; Q54RF5; -. DR SMR; Q54RF5; -. DR STRING; 44689.Q54RF5; -. DR PaxDb; 44689-DDB0231421; -. DR EnsemblProtists; EAL65862; EAL65862; DDB_G0283247. DR GeneID; 8623966; -. DR KEGG; ddi:DDB_G0283247; -. DR dictyBase; DDB_G0283247; pyk. DR eggNOG; KOG2323; Eukaryota. DR HOGENOM; CLU_015439_0_2_1; -. DR InParanoid; Q54RF5; -. DR OMA; MVRVHHL; -. DR PhylomeDB; Q54RF5; -. DR Reactome; R-DDI-6798695; Neutrophil degranulation. DR Reactome; R-DDI-70171; Glycolysis. DR UniPathway; UPA00109; UER00188. DR PRO; PR:Q54RF5; -. DR Proteomes; UP000002195; Chromosome 4. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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. PE 1: Evidence at protein level; KW ATP-binding; Direct protein sequencing; Glycolysis; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Potassium; Pyruvate; Reference proteome; KW Transferase. FT CHAIN 1..507 FT /note="Pyruvate kinase" FT /id="PRO_0000327689" FT BINDING 50 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 52..55 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 52 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 54 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 84 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 85 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 177 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 242 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 265 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 266 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 266 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 298 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 240 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 507 AA; 54999 MW; AC93DBF9A53B705D CRC64; MATLSRNLRL SLDTPTSTFV RTKIVCTIGP KTMSEEALIK LIETGMNVCR LNFSHGTHDY HGQVIKNVRS AMEKTGKIIA IMLDTKGPEI RTGKIEDRCG YVDLFVGQEI LVDTNMNQPG TSFRISIDYK GLLDSVKVGG YILIADGVIS LSITAVEKEK GHVVCRVNNN SRLGENKNVH LPGAIVNLPA VSEKDILDIK FGVEQNVDFI AASFIRKADD VNEIREILGE KGKDIQIISK IENVEGVDNF NEILEVSDGI MVARGDLGVE VQMEKIFVAQ KMIVSKCNAA GKPVITATQM LESMIKNPRP TRAEATDVAN AVLDGSDCVM LSGETASGDY PYEAVDIMAK ICREAELVES STDYQTLFAA LKLSSAKPVS IAETVASYAV ATAIDLKADL IITLTETGLT ARLVSKYRPS IPIIAVTSWS YTVKHLLATR GAIPFLVESL VGTDKLVESC LEYAMKHNLC KKGSRVVIVS GVMEGVPGKT NSLRVLTVGE SIKDLKV //