ID KPYK_METEA Reviewed; 478 AA. AC O05118; C5AUT3; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 2. DT 27-MAR-2024, entry version 139. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; Synonyms=pykA; OrderedLocusNames=MexAM1_META1p2941; OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB OS 9133 / AM1) (Methylobacterium extorquens). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Methylobacteriaceae; Methylorubrum. OX NCBI_TaxID=272630; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Chistoserdova L., Lidstrom M.E.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1; RX PubMed=19440302; DOI=10.1371/journal.pone.0005584; RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y., RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W., RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E., RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D., RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J., RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C., RA Lidstrom M.E.; RT "Methylobacterium genome sequences: a reference blueprint to investigate RT microbial metabolism of C1 compounds from natural and industrial sources."; RL PLoS ONE 4:E5584-E5584(2009). 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 -!- SEQUENCE CAUTION: CC Sequence=AAB66498.1; Type=Erroneous initiation; Evidence={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; U87316; AAB66498.1; ALT_INIT; Genomic_DNA. DR EMBL; CP001510; ACS40693.1; -; Genomic_DNA. DR RefSeq; WP_003601864.1; NC_012808.1. DR AlphaFoldDB; O05118; -. DR SMR; O05118; -. DR STRING; 272630.MexAM1_META1p2941; -. DR GeneID; 72990392; -. DR KEGG; mea:Mex_1p2941; -. DR eggNOG; COG0469; Bacteria. DR HOGENOM; CLU_015439_0_2_5; -. DR OrthoDB; 9812123at2; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000009081; Chromosome. 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; 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; PYRUVATE KINASE; 1. DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 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; Potassium; Pyruvate; Reference proteome; Transferase. FT CHAIN 1..478 FT /note="Pyruvate kinase" FT /id="PRO_0000112078" FT BINDING 35 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 37..40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 37 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 39 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 76 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 157 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 219 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 242 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 243 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 243 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 275 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 217 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT CONFLICT 60 FT /note="A -> G (in Ref. 1; AAB66498)" FT /evidence="ECO:0000305" FT CONFLICT 165 FT /note="V -> A (in Ref. 1; AAB66498)" FT /evidence="ECO:0000305" SQ SEQUENCE 478 AA; 51801 MW; 6C58142F1B17E3AA CRC64; MKRSRRTKIV ATLGPASDTP EMIEKLFHAG ADVFRINMSH LAREKLPERI EVIRTIEREA KRPIGILVDL QGPKLRLGTF VGDAAVLENG QTFVLDSDPT PGDTDRVFLP HPEILSALEP SHGILIDDGK LRLIVTEVSE GRAVTRVEVG GRISNRKGVS LPHTVLPVPA MTEKDRGDLE AGLAAGADWI AVSFVQRPED VAEVKKVAAG RALVMAKIEK PQALTRLDEI IEISDGIMVA RGDLGVEMPL EQVPGVQKRI TRVARRLGKP VVVATQMLES MITSPVPTRA EVSDVATAVY EGADAVMLSA ESAAGDFPVE AIGTMNRIAE QVERDALYWS ILMAQRSEPE PTASDAIAAA AHQIVEALSL RSIMAWTHSG STVLRLARAR PNASVIALTP KRETARRLTM AWGVHPIVTK DASDVDDMAF RAAKFAVRER FAEIGDRVII VAGVPFGIPG ATNMVRIAFV TREHAERA //