ID KPYK_EMENI Reviewed; 526 AA. AC P22360; C8VF86; Q5B2M0; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 26-FEB-2020, entry version 140. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pkiA; Synonyms=pki; ORFNames=AN5210; OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / OS M139) (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=227321; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=WG096; RX PubMed=3072099; DOI=10.1007/bf00434080; RA de Graaff L., Visser J.; RT "Structure of the Aspergillus nidulans pyruvate kinase gene."; RL Curr. Genet. 14:553-560(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(2005). RN [3] RP GENOME REANNOTATION. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003; RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K., RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J., RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., RA Oliver S.G., Turner G.; RT "The 2008 update of the Aspergillus nidulans genome annotation: a community RT effort."; RL Fungal Genet. Biol. 46:S2-13(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 -!- ACTIVITY REGULATION: Regulated by phosphoenolpyruvate substrate and CC allosteric effectors such as fructose 1,6 diphosphate and magnesium. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. 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; M36918; AAA33320.1; -; Genomic_DNA. DR EMBL; AACD01000089; EAA62391.1; -; Genomic_DNA. DR EMBL; BN001305; CBF81089.1; -; Genomic_DNA. DR PIR; S27364; S27364. DR RefSeq; XP_662814.1; XM_657722.1. DR SMR; P22360; -. DR STRING; 162425.CADANIAP00003208; -. DR PRIDE; P22360; -. DR EnsemblFungi; CBF81089; CBF81089; ANIA_05210. DR EnsemblFungi; EAA62391; EAA62391; AN5210.2. DR GeneID; 2871501; -. DR KEGG; ani:AN5210.2; -. DR HOGENOM; CLU_015439_0_1_1; -. DR InParanoid; P22360; -. DR KO; K00873; -. DR OMA; QVPIVQK; -. DR OrthoDB; 933620at2759; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000000560; Chromosome V. DR Proteomes; UP000005890; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0061621; P:canonical glycolysis; IEA:EnsemblFungi. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR GO; GO:0042866; P:pyruvate biosynthetic process; IEA:EnsemblFungi. DR CDD; cd00288; Pyruvate_Kinase; 1. 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; 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 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. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium; Pyruvate; KW Reference proteome; Transferase. FT CHAIN 1..526 FT /note="Pyruvate kinase" FT /id="PRO_0000112113" FT NP_BIND 65..68 FT /note="ATP" FT /evidence="ECO:0000250|UniProtKB:P14618" FT METAL 65 FT /note="Potassium" FT /evidence="ECO:0000250" FT METAL 67 FT /note="Potassium" FT /evidence="ECO:0000250" FT METAL 98 FT /note="Potassium" FT /evidence="ECO:0000250" FT METAL 99 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000250" FT METAL 256 FT /note="Magnesium" FT /evidence="ECO:0000255" FT METAL 280 FT /note="Magnesium" FT /evidence="ECO:0000250" FT BINDING 63 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 105 FT /note="ATP" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 191 FT /note="ATP" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 279 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000250" FT BINDING 280 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000250" FT BINDING 312 FT /note="Substrate" FT /evidence="ECO:0000250" FT SITE 254 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0000255" FT CONFLICT 88 FT /note="Q -> A (in Ref. 1; AAA33320)" FT /evidence="ECO:0000305" SQ SEQUENCE 526 AA; 58133 MW; BCD3A6F35F5D28B2 CRC64; MAASSSLDHL SNRMKLEWHS KLNTEMVPAK NFRRTSIICT IGPKTNSVEK INALRRAGLN VVRMNFSHGS YEYHQSVIDH AREAEKQQAG RPVAIALDTK GPEIRTGNTV GDKDIPIKAG HEMNISTDEQ YATASDDQNM YVDYKNITKV ISAGKLIYVD DGILSFEVLE VVDDKTLRVR CLNNGNISSR KGVNLPGTDV DLPALSEKDI SDLKFGVKNK VDMVFASFIR RGSDIRHIRE VLGEEGREIQ IIAKIENQQG VNNFDEILEE TDGVMVARGD LGIEIPAPKV FIAQKMMIAK CNIKGKPVIC ATQMLESMTY NPRPTRAEVS DVANAVLDGA DCVMLSGETA KGNYPCEAVT MMSETCLLAE VAIPHFNVFD ELRNLAPRPT DTVESIAMAA VSASLELNAG AIVVLTTSGN TARMISKYRP VCPIIMVSRN PAATRYSHLY RGVWPFYFPE KKPDFNVKIW QEDVDRRLKW GINHGLKLGI INKGDNIVCV QGWRGGMGHT NTVRVVPAEE NLGLSE //