ID A8MR07_ARATH Unreviewed; 474 AA. AC A8MR07; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 07-OCT-2020, entry version 115. DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504}; DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504}; GN OrderedLocusNames=At3g52990 {ECO:0000313|Araport:AT3G52990, GN ECO:0000313|EMBL:AEE79023.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702 {ECO:0000313|EMBL:AEE79023.1, ECO:0000313|Proteomes:UP000006548}; RN [1] {ECO:0000313|EMBL:AEE79023.1, ECO:0000313|Proteomes:UP000006548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=11130713; DOI=10.1038/35048706; RG European Union Chromosome 3 Arabidopsis Sequencing Consortium; RG Institute for Genomic Research; RG Kazusa DNA Research Institute; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(2000). RN [2] {ECO:0000313|EMBL:BAH20134.1} RP NUCLEOTIDE SEQUENCE. RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., RA Shinozaki K.; RT "Analysis of multiple occurrences of alternative splicing events in RT Arabidopsis thaliana using novel sequenced full-length cDNAs."; RL DNA Res. 0:0-0(2009). RN [3] {ECO:0000313|EMBL:AEE79023.1} RP NUCLEOTIDE SEQUENCE. RG TAIR; RA Swarbreck D., Lamesch P., Wilks C., Huala E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:AEE79023.1} RP GENOME REANNOTATION. RA Lavstsen T., Jespersen J.S.; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|Proteomes:UP000006548} RP GENOME REANNOTATION. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). 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; Evidence={ECO:0000256|ARBA:ARBA00001174, CC ECO:0000256|RuleBase:RU000504}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|ARBA:ARBA00001958}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997, CC ECO:0000256|RuleBase:RU000504}. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}. 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; CP002686; AEE79023.1; -; Genomic_DNA. DR EMBL; AK317468; BAH20134.1; -; mRNA. DR RefSeq; NP_001078275.1; NM_001084806.1. DR SMR; A8MR07; -. DR PRIDE; A8MR07; -. DR ProteomicsDB; 181476; -. DR EnsemblPlants; AT3G52990.2; AT3G52990.2; AT3G52990. DR GeneID; 824465; -. DR Gramene; AT3G52990.2; AT3G52990.2; AT3G52990. DR KEGG; ath:AT3G52990; -. DR Araport; AT3G52990; -. DR HOGENOM; CLU_015439_9_1_1; -. DR KO; K00873; -. DR OMA; QGQEASN; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; A8MR07; baseline and differential. 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 Gene3D; 2.40.33.10; -; 1. DR Gene3D; 3.20.20.60; -; 1. DR Gene3D; 3.40.1380.20; -; 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; 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 PANTHER; PTHR11817; PTHR11817; 1. DR Pfam; PF00224; PK; 1. DR Pfam; PF02887; PK_C; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR SUPFAM; SSF50800; SSF50800; 1. DR SUPFAM; SSF51621; SSF51621; 1. DR SUPFAM; SSF52935; SSF52935; 1. DR TIGRFAMs; TIGR01064; pyruv_kin; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000504}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000504, KW ECO:0000313|EMBL:AEE79023.1}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Proteomics identification {ECO:0000213|ProteomicsDB:A8MR07}; KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:AEE79023.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006548}; KW Transferase {ECO:0000256|RuleBase:RU000504}. FT DOMAIN 1..322 FT /note="PK" FT /evidence="ECO:0000259|Pfam:PF00224" FT DOMAIN 342..469 FT /note="PK_C" FT /evidence="ECO:0000259|Pfam:PF02887" SQ SEQUENCE 474 AA; 51890 MW; 9CA4A736DC1C7E96 CRC64; MSVARFDFSW GDADYHQETL DNLKVAVRST KKLCAVMLDT VGPELQVINK SEKAITLKAD GLVTLTPNQD QEASSEVLPI NFNGLAKAVK KGDTIFVGQY LFTGSETTSV WLEVDEVKGD DVICLSRNAA TLAGSLFTLH SSQVHIDLPT LTEKDKEVIS TWGVQNKIDF LSLSYCRHAE DVRQTREMLK KLGDLSQTQI FAKIENVEGL THFDEILQEA DGIILSRGNL GIDLPPEKVF LFQKAALYKC NMAGKPAVLT RVVDSMTDNL RPTRAEATDV ANAVLDGSDA ILLGAETLRG LYPVETISTV GRICAEAEKV FNQDLYFKKT VKYVGEPMTH LESIASSAVR AAIKVKASVI ICFTSSGRAA RLIAKYRPTM PVISVVIPRV KTNQLKWSFS GAFEARQSLI VRGLFPMLAD PRHPAESTSA TNESVLKVAL DHGKHAGVIK SHDRVVVCQK VGDASVVKII ELED //