ID KPYK2_TRYBB Reviewed; 499 AA. AC P30616; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 13-SEP-2023, entry version 104. DE RecName: Full=Pyruvate kinase 2; DE Short=PK 2; DE EC=2.7.1.40; GN Name=PYK2; OS Trypanosoma brucei brucei. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=427; RX PubMed=1879424; DOI=10.1111/j.1432-1033.1991.tb21043.x; RA Allert S., Ernest I., Poliszczak A., Opperdoes F.R., Michels P.A.M.; RT "Molecular cloning and analysis of two tandemly linked genes for pyruvate RT kinase of Trypanosoma brucei."; RL Eur. J. Biochem. 200:19-27(1991). 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 -!- ACTIVITY REGULATION: Activated by fructose 2,6-bisphosphate, activated CC by the effector in a cooperative manner. 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; X57951; CAA41019.1; -; Genomic_DNA. DR PIR; S17649; S17649. DR AlphaFoldDB; P30616; -. DR SMR; P30616; -. DR SABIO-RK; P30616; -. 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 Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Potassium; Pyruvate; Transferase. FT CHAIN 1..499 FT /note="Pyruvate kinase 2" FT /id="PRO_0000112104" 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 241 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255" FT BINDING 264 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 265 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 297 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 239 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 499 AA; 54452 MW; 7FE8238E73E45CA2 CRC64; MSQLEHNIGL SIFEPVAKHR ANRIVCTIGP STQSVEALKN LMKSGMSVAR MNFSHGSHEY HQTTINNVRA AAAELGLHIG IALDTKGPEI RTGLFKDGEV TFAPGDIVCV TTDPAYEKVG TKEKFYIDYP QLTKAVPVGG SIYVDDGVMT LRVLSKEDDR TLKCHVNNHH RLTDRRGINL PGCEVDLPAV SEKDRKDLEF GVAQGVDMIF ASFIRTAEQV REVRAALGEK GKDILIISKI ENHQGVQNID SIIEASNGIM VARGDLGVEI PAEKVCVAQM CIISKCNVVG KPVICATQML ESMTSNPRPT RAEVSDVANA VLNGADCVML SGETAKGKYP NEVVQYMARI CVEAQSATHD TVMFNSIKNL QKIPMCPEEA VCSSAVASAF EVQAKAMLVL SNTGRSARLI SKYRPNCPII CVTTRLQTCR QLNVTRSVVS VFYDAAKSGE DKDKEKRVKL GLDFAKKEKY ASTGDVVVVV HADHSVKGYP NQTRLIYLP //