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Database: UniProt
Entry: A0A3M6VPK5_9STRA
LinkDB: A0A3M6VPK5_9STRA
Original site: A0A3M6VPK5_9STRA 
ID   A0A3M6VPK5_9STRA        Unreviewed;       505 AA.
AC   A0A3M6VPK5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   ORFNames=DD238_005629 {ECO:0000313|EMBL:RMX68644.1};
OS   Peronospora effusa.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Peronospora.
OX   NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX68644.1, ECO:0000313|Proteomes:UP000282087};
RN   [1] {ECO:0000313|EMBL:RMX68644.1, ECO:0000313|Proteomes:UP000282087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R14 {ECO:0000313|EMBL:RMX68644.1,
RC   ECO:0000313|Proteomes:UP000282087};
RA   Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA   Reyes Chin-Wo S., Mou B., Michelmore R.;
RT   "Comparative genomics of downy mildews reveals potential adaptations to
RT   biotrophy.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RMX68644.1}.
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DR   EMBL; QLLG01000060; RMX68644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M6VPK5; -.
DR   STRING; 542832.A0A3M6VPK5; -.
DR   VEuPathDB; FungiDB:DD237_004560; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000282087; Unassembled WGS sequence.
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: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   3: Inferred from homology;
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282087};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          26..350
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          388..502
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   505 AA;  54519 MW;  6DEAABEC3AACB98A CRC64;
     MSGALGLSQQ GVELESIMRS TEGIARKTRI FCTVGPTCWS KEGLAELIDA GMNLARFNFS
     HGDHSSHAEA LDRLRTVLAT RPYKNIATML DTKGPEIRTG FLANKEKVHI KKGSILELTT
     DYDFLGDETK IACSYPELPQ SVKIGGTILI ADGSLVLTVT EIKDDSVVTR ANNAAMLSER
     KNMNLPGCKV MLPTLTEKDK DDLVNFGLVH GIDYIAASFV RAGQDIDNIR KVLGPRGRGI
     KIIAKIENQE GLENFDEILA KTDGVMVARG DLGMEIPPEK VFLAQKMMIR KANIAGKPVV
     TATQMLESMI KAPRPTRAEC TDVANAVLDG TDAVMLSGET ANGNYATEAV TMMSKICVQA
     EGAIHYNELY QALHNSVLDT YGQMDILEAI TSSAVKTAID IDAKMIVVLT ESGNTARLVS
     KFRPSMPVLV LTAVGATARQ SEGFNKGVTA RCMGSMIGTE SILFRATDLG KQFGWLEPGD
     NVVALHGMVE ARSGSTNMLK VLTVE
//
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