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Database: UniProt
Entry: F8AJ25_PYRYC
LinkDB: F8AJ25_PYRYC
Original site: F8AJ25_PYRYC 
ID   F8AJ25_PYRYC            Unreviewed;       476 AA.
AC   F8AJ25;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   OrderedLocusNames=PYCH_07870 {ECO:0000313|EMBL:AEH24472.1};
OS   Pyrococcus yayanosii (strain CH1 / JCM 16557).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=529709 {ECO:0000313|EMBL:AEH24472.1, ECO:0000313|Proteomes:UP000008386};
RN   [1] {ECO:0000313|EMBL:AEH24472.1, ECO:0000313|Proteomes:UP000008386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH1 / JCM 16557 {ECO:0000313|Proteomes:UP000008386};
RX   PubMed=21705594; DOI=10.1128/JB.05345-11;
RA   Jun X., Lupeng L., Minjuan X., Oger P., Fengping W., Jebbar M., Xiang X.;
RT   "Complete genome sequence of the obligate piezophilic hyperthermophilic
RT   archaeon Pyrococcus yayanosii CH1.";
RL   J. Bacteriol. 193:4297-4298(2011).
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|ARBA:ARBA00004997,
CC       ECO:0000256|RuleBase:RU000504}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR   EMBL; CP002779; AEH24472.1; -; Genomic_DNA.
DR   RefSeq; WP_013905529.1; NC_015680.1.
DR   AlphaFoldDB; F8AJ25; -.
DR   STRING; 529709.PYCH_07870; -.
DR   GeneID; 10837362; -.
DR   KEGG; pya:PYCH_07870; -.
DR   eggNOG; arCOG04120; Archaea.
DR   HOGENOM; CLU_015439_0_2_2; -.
DR   OrthoDB; 56298at2157; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000008386; Chromosome.
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, ECO:0000313|EMBL:AEH24472.1};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          6..327
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          364..472
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   476 AA;  52957 MW;  06000AC1AC15188E CRC64;
     MKLPPQKTKI VATIGPATKS KRMIEKLIKA GMSVARINFS HGTFEEHAKV IEAVREASQK
     LDRRVAILAD LPGLKIRVGE IKGSYVELRR GDKVILTTRD VEGDGMVIPV EYKDFPRLVS
     KGDTIYLSDG YIVLKVEEVR DTDVEALVIS GGKLFSRKGI NIPKAHLPVE AVTPRDMEII
     EFAIEHGVDA IGISFVGSVY DVLKVKRFLE KKGAGNVFVV AKIERPDAVR NFDEILNAAD
     AIMIARGDLG VEMPIERLPI LQKQLIRKAN VQGKPVITAT QMLVSMTTEK VPTRAEVTDV
     ANAILDGTDA VMLSEETAVG KFPVEAVEMM VKIAKVTEEY RESFGMVRMR EFMEITPQKG
     AIKEAITRSI VDALCTVNIK YILTPTRTGR TPRLISRFKP KQWILAFSTD ERVCNNLMFS
     YGVYPFCMEE DFDERDIVRL IKGLGLVQSD DIVLMTEGKP IEKTVGTNSI KIFTIA
//
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