ID A0A6A4FJA1_9STRA Unreviewed; 599 AA.
AC A0A6A4FJA1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=PR002_g8669 {ECO:0000313|EMBL:KAE9033433.1}, PR003_g8514
GN {ECO:0000313|EMBL:KAE9344354.1};
OS Phytophthora rubi.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=129364 {ECO:0000313|EMBL:KAE9344354.1, ECO:0000313|Proteomes:UP000434957};
RN [1] {ECO:0000313|EMBL:KAE9344354.1, ECO:0000313|Proteomes:UP000434957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRP324 {ECO:0000313|EMBL:KAE9033433.1,
RC ECO:0000313|Proteomes:UP000435112}, and SCRP333
RC {ECO:0000313|EMBL:KAE9344354.1, ECO:0000313|Proteomes:UP000434957};
RA Adams T.M., Armitage A.D., Sobczyk M.K., Bates H.J., Dunwell J.M.,
RA Nellist C.F., Harrison R.J.;
RT "Genomic investigation of the strawberry pathogen Phytophthora fragariae
RT indicates pathogenicity is determined by transcriptional variation in three
RT key races.";
RL Submitted (AUG-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:KAE9344354.1}.
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DR EMBL; QXFU01000444; KAE9033433.1; -; Genomic_DNA.
DR EMBL; QXFT01000424; KAE9344354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A4FJA1; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000434957; Unassembled WGS sequence.
DR Proteomes; UP000435112; 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; 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.
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, ECO:0000313|EMBL:KAE9344354.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000434957};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 100..424
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 459..573
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 65132 MW; D748EA37C89E8B35 CRC64;
MSERHGSARN PRTGTVMHSL PRRRSKDDEL MRTPSSAYDQ LRVSGFPPVR LGSWHRYRSL
SQEFDDVFKP ESSSIVRKPA NFHVGIELKQ IMTPTTARAR KTKIICAIGP ASWSVEMLGQ
LLDAGMNVAR LNFSHGDHEL HMRSLSNLRE AMAARPGCHC AVLLDTKGPE IRSGFLKGHT
PVQLKAGQTL EITTDYGVEG DSSRIACTYE QLPTSVSVGS KILCDDGSLV MTVIECRPES
IVVRVHNDHL LEEKKNMNLP GAAIQIPGIT EKDEDDLLNF AIPNGVDIVS GSFVRSAANV
RAIRECLGED GRHIRVHAKI ESQEALQNID EIIAEADGIH VSRGDLGMEL SPERVFLAQK
MIIGKANRAG KPVVTSTQML QSMTKKIIPS NAECTDVANA VLDGTDAMML SAETAKGMYP
KEAVATMAKI CIEAEQALDY AEVYRLHRAA NNKNVSMCES VASSAVEISI DMDVKLIISI
TDSGDSTKLL AKYRPKANIV AVTSSTLTAR QLSGVSRGVT ALLVDSMTDV DDLTLQAIAF
AKERGLIKSG DVVILVHGLD DAVSKSTNVV KVIEVDKQSC SSYSSPKHSF FSGIHIPFT
//
