ID   A0A097IU65_9PHAE        Unreviewed;       503 AA.
AC   A0A097IU65;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-NOV-2024, entry version 36.
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   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=pyruvate + ATP = phosphoenolpyruvate + ADP + H(+);
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC       ECO:0000256|RuleBase:RU000504}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR   EMBL; KM113630; AIT69998.1; -; mRNA.
DR   UniPathway; UPA00109; UER00188.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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   FunFam; 2.40.33.10:FF:000001; Pyruvate kinase; 1.
DR   FunFam; 3.20.20.60:FF:000001; Pyruvate kinase; 1.
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:SF3; AT14039P-RELATED; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 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   2: Evidence at transcript 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   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:AIT69998.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          24..348
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          386..500
FT                   /note="Pyruvate kinase C-terminal"
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
//