KPYK_THELN
ID KPYK_THELN Reviewed; 475 AA.
AC Q56301; H3ZJK4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pki; ORFNames=OCC_05009;
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=22493191; DOI=10.1128/jb.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-216.
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=7642512; DOI=10.1128/jb.177.16.4817-4819.1995;
RA Kletzin A., Mukund S., Kelley-Crouse T.L., Chan M.K.S., Rees D.C.,
RA Adams M.W.W.;
RT "Molecular characterization of the genes encoding the tungsten-containing
RT aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and
RT formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis.";
RL J. Bacteriol. 177:4817-4819(1995).
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;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA58793.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP006670; EHR79867.1; -; Genomic_DNA.
DR EMBL; X83963; CAA58793.1; ALT_INIT; Genomic_DNA.
DR PIR; A57418; A57418.
DR RefSeq; WP_004066098.1; NC_022084.1.
DR AlphaFoldDB; Q56301; -.
DR SMR; Q56301; -.
DR STRING; 523849.OCC_05009; -.
DR EnsemblBacteria; EHR79867; EHR79867; OCC_05009.
DR GeneID; 16548766; -.
DR KEGG; tlt:OCC_05009; -.
DR HOGENOM; CLU_015439_0_2_2; -.
DR OMA; QVPIVQK; -.
DR OrthoDB; 40634at2157; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000015502; 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 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 3: Inferred from homology;
KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Transferase.
FT CHAIN 1..475
FT /note="Pyruvate kinase"
FT /id="PRO_0000112130"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 38..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 38
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 221
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 23
FT /note="T -> S (in Ref. 2; CAA58793)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 52767 MW; 7970729B9948B94A CRC64;
MELPSHKTKI IATIGPASKQ KETIKKMIKA GMSVARINFS HGTLEEHAKT IETVRDVAEK
LERRVAILGD LPGLKMRVGK IKGDSVTLRK GDKVVLTTRD IEGDETTIPV EFKDLPKLVS
KGDTIYLSDG YIMLRVEEVR ENEVECVVVN GGILFSHKGI NIPKANLPIE AITPRDFEII
EFAIEHGVDA IGLSFVGSVY DVLKVKSFLE KKSADLFVIA KIERPDAVRN FDEILNAADG
IMIARGDLGV EMPIEKLPIM QKQLIKKTNL AAKPVITATQ MLVSMTTERI PKRAEVTDVA
NAILDGTDAV MLSEETAIGK YPVESVEMMA KIAKTTEEYR ESLGYSRLRA WIDSLPKRST
IKEAITRSVI DALCAIDIKY ILTPTRTGLT PRLISRFKPK QWILAFSSSE RVCNNLAFSY
GVYPFCMDEN FNEKDIIMLV KGLGIVKEDD TVLLTEGRPI GKTVGTNTMR IFQIP
