ID KPYK_SPOPS Reviewed; 586 AA. AC P51182; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-SEP-2023, entry version 110. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OS Sporosarcina psychrophila (Bacillus psychrophilus). OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina. OX NCBI_TaxID=1476; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7549104; DOI=10.1271/bbb.59.1536; RA Tanaka K., Sakai H., Ohta T., Matsuzawa H.; RT "Molecular cloning of the genes for pyruvate kinase of two bacilli, RT Bacillus psychrophilus and Bacillus licheniformis, and comparison of the RT properties of the enzymes produced in Escherichia coli."; RL Biosci. Biotechnol. Biochem. 59:1536-1542(1995). 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 -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PEP-utilizing CC enzyme 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; D31954; BAA06725.1; -; Genomic_DNA. DR PIR; JC4219; JC4219. DR RefSeq; WP_067207646.1; NZ_CP014616.1. DR AlphaFoldDB; P51182; -. DR SMR; P51182; -. DR STRING; 1476.AZE41_07700; -. DR OrthoDB; 9812123at2; -. DR BRENDA; 2.7.1.40; 685. 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 Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1. DR Gene3D; 3.50.30.10; Phosphohistidine domain; 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; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR036637; Phosphohistidine_dom_sf. 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; PF00391; PEP-utilizers; 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; SSF52009; Phosphohistidine 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; Potassium; Pyruvate; Transferase. FT CHAIN 1..586 FT /note="Pyruvate kinase" FT /id="PRO_0000112054" FT BINDING 32 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 34..37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 34 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 36 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 66 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 67 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 156 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 222 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 245 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 246 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 246 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 278 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 220 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 586 AA; 62571 MW; 8C0B7017C9C6D5CE CRC64; MRKTKIVCTI GPASESPELL EQLIEAGMNV ARLNFSHGNH AEHKARIDSI RKVAREKGKV VGILLDTKGP EIRTHSMMNG KLELVTGQKI DISMTQVEGN NDVFSVSYDK LIEDVNEGSV ILLDDGLIQL EVTGKDVARG LIHTLIINSG SLSNNKGVNI PGVSVQLPGM TEKDAEDILF GIREGVDFIA ASFVRRASDV MEIRALLENN NGSNLQIIPK IENQEGVDNI DEILNVSDGL MVARGDLGVE IPPEEVPLVQ KNLIEKCNQA GKPVITATQM LDSMQRNPRP TRAEASDVAN AIFDGTDAIM LSGETAAGIY PVESVQTMDR IALTTEAAID YRSVVSTRRR EKHGNMTEAI GQAAAYTAIN LKVKAVLAPT ESGHTAKMIA KYRPGCPVIA VTSSEMCSRK LSLIWGVYPI VGKKASSIDE ILQESVEESV KHQYVGHGDV VIITAGVPVG EAGTTNLMKI HVIGDLLARG QGIGKDVAYG RTVVAKNAAE ALAYDTEGAI LVTNASDRDM MPAIEKCAGL ITEEGGLTSH GAIVGLSLGI PIIVGVENAT ELIQHGKEIT MDAESGVIYN GHASVL //