ID KPYK_HYPJE Reviewed; 538 AA. AC P31865; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 13-SEP-2023, entry version 120. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pki1; OS Hypocrea jecorina (Trichoderma reesei). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma. OX NCBI_TaxID=51453; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8359694; DOI=10.1016/0378-1119(93)90430-b; RA Schindler M., Mach R.L., Vollenhofer S.K., Hodits R., Gruber F., Visser J., RA de Graaff L., Kubicek C.P.; RT "Characterization of the pyruvate kinase-encoding gene (pki1) of RT Trichoderma reesei."; RL Gene 130:271-275(1993). 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; L07060; AAA02922.1; -; Unassigned_DNA. DR PIR; JN0780; JN0780. DR AlphaFoldDB; P31865; -. DR SMR; P31865; -. DR VEuPathDB; FungiDB:TrQ_002335; -. DR OMA; RVHHIGE; -. DR UniPathway; UPA00109; UER00188. 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; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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. PE 3: Inferred from homology; KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Potassium; Pyruvate; Transferase. FT CHAIN 1..538 FT /note="Pyruvate kinase" FT /id="PRO_0000112119" FT BINDING 72 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 74..77 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 74 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 76 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 107 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 108 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 114 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 200 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 265 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 288 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 289 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 289 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 321 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 263 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0000255" SQ SEQUENCE 538 AA; 58888 MW; E9C26AC0E8186FE7 CRC64; MSQISRTQSI MATTAQEHLE TGGRINWLAS LNTAFTPARN FRRTSIICTI GPKTNSVEAL NKLRDAGLNV ARMNFSHGSY EYHQSVIDNV RASVAAHPGR PVAIALDTKG PEIRTGNTAG DVDIPISAGT VMNFTTDEKY ATACDTQNMY VDYKNITKVI QPGRVIYVDD GVLAFDVLSI KDDQTVEVRA RNNGFISSRK GVNLPNTDVD LPALSEKDKA DLRFGVKNNV DMVFASFIRR AQDIKDIRDV LGPEGKQIQI IAKIENRQGL NNFAEILEET DGVMVARGDL GIEIPAAEVF AAQKKMIAMC NIAGKPVICA TQMLESMIKN PRPTRAEISD VGNAVTDGAD CVMLSGETAK GNYPAESIHE MHEASLKAEN TIPYVSHFEE MCTLVKRPVS TVESCAMAAV RASLDLGAGG IIVLSTSGDS ARLLSKYRPV CPIFMVTRNP TTSRFSHLYR GVYPFLYPEQ KPDFDTVNWQ EDVDKRIKWA VTRAIELKTL TAGDTVVVVQ GWKGGMGNTN TLRIVRADPD HLGIGQME //