ID A0A097IU65_9PHAE Unreviewed; 503 AA. AC A0A097IU65; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 22-APR-2020, entry version 20. DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504}; DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504}; GN Name=pk {ECO:0000313|EMBL:AIT69998.1}; OS Colpomenia sinuosa. OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae; OC Ectocarpales; Scytosiphonaceae; Colpomenia. OX NCBI_TaxID=87236 {ECO:0000313|EMBL:AIT69998.1}; RN [1] {ECO:0000313|EMBL:AIT69998.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=QLMZ-2014531 {ECO:0000313|EMBL:AIT69998.1}; RX PubMed=25313828; RA Chi S., Wu S., Yu J., Wang X., Tang X., Liu T.; RT "Phylogeny of c4-photosynthesis enzymes based on algal transcriptomic and RT genomic data supports an archaeal/proteobacterial origin and multiple RT duplication for most c4-related genes."; RL PLoS ONE 9:E110154-E110154(2014). 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|RuleBase:RU000504}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|RuleBase:RU000504}. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. CC {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; KM113630; AIT69998.1; -; mRNA. DR UniPathway; UPA00109; UER00188. 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; 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 2: Evidence at transcript level; KW Glycolysis {ECO:0000256|RuleBase:RU000504}; KW Kinase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:AIT69998.1}; KW Magnesium {ECO:0000256|RuleBase:RU000504}; KW Pyruvate {ECO:0000313|EMBL:AIT69998.1}; KW Transferase {ECO:0000256|RuleBase:RU000504}. FT DOMAIN 24..365 FT /note="PK" FT /evidence="ECO:0000259|Pfam:PF00224" FT DOMAIN 386..500 FT /note="PK_C" FT /evidence="ECO:0000259|Pfam:PF02887" SQ SEQUENCE 503 AA; 54631 MW; F0A1403FEBFF0CF2 CRC64; MAQLLRGSNI SQDKIFTDCD ESRRKCKIIC TLGPACWSVE TLGALVDAGM NVARLNFSHG DHEGHAATLQ RLRQAXXXXX XXXVAVLLDT KGPEIRTGFL ANKKSAELTR GQDLELTTDY EFLGDNTKIA CSYKSLPTSV KAGSKILVAD GSLVLTVKEC KETSVICEVM NNCVLGERKN MNLPGAIVDL PTLTEKDIDD LQNFGLVHQV DYIAASFVRK PEDIDTIRMV LGEEGANIKI IAKIENQEGI RNYDQILLKT DAIMVARGDM GMEIPPEKVF LAQKYMIRRA NIAGKPVVTA TQMLESMIKN PRPTRAECTD VANAVLDGTD CVMLSGETAN GDYPVDAVTM MSRTCCEAEC ALNYDSLYQA TRNTVMREFE SMEPAESVAS SAVKTAIDLN AAMVVVLTET GTTARLLAKY RPDMPILAFT AAADAARQMN GYLRNVTSQV IGSMIGTDSI VFRAIDIGKQ NGWVKPGDKV VCIHGMKEAT AGSTNSMRVI VAA //