ID   KPYK_AERPE              Reviewed;         458 AA.
AC   Q9YEU2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   Name=pyk; OrderedLocusNames=APE_0489;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
RN   [2]
RP   BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, AND REGULATION.
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=12654928; DOI=10.1074/jbc.m210288200;
RA   Johnsen U., Hansen T., Schoenheit P.;
RT   "Comparative analysis of pyruvate kinases from the hyperthermophilic
RT   archaea Archaeoglobus fulgidus, Aeropyrum pernix, and Pyrobaculum
RT   aerophilum and the hyperthermophilic bacterium Thermotoga maritima: unusual
RT   regulatory properties in hyperthermophilic archaea.";
RL   J. Biol. Chem. 278:25417-25427(2003).
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:0000269|PubMed:12654928};
CC   -!- ACTIVITY REGULATION: Not activated by classical allosteric effectors.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=53 umol/min/mg enzyme (at 65 degrees Celsius)
CC         {ECO:0000269|PubMed:12654928};
CC       pH dependence:
CC         Optimum pH is 6.1. {ECO:0000269|PubMed:12654928};
CC       Temperature dependence:
CC         Optimum temperature is higher than 95 degrees Celsius. Still active
CC         after 120 minutes at 100 degrees Celsius.
CC         {ECO:0000269|PubMed:12654928};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12654928}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR   EMBL; BA000002; BAA79454.1; -; Genomic_DNA.
DR   PIR; B72745; B72745.
DR   AlphaFoldDB; Q9YEU2; -.
DR   SMR; Q9YEU2; -.
DR   STRING; 272557.APE_0489; -.
DR   EnsemblBacteria; BAA79454; BAA79454; APE_0489.
DR   KEGG; ape:APE_0489; -.
DR   PATRIC; fig|272557.25.peg.372; -.
DR   eggNOG; arCOG04120; Archaea.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000002518; 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; IPR015793; Pyrv_Knase_brl.
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   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   1: Evidence at protein level;
KW   ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT   CHAIN           1..458
FT                   /note="Pyruvate kinase"
FT                   /id="PRO_0000295180"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         35..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         35
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            212
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   458 AA;  50487 MW;  3D8E11A37A0088E3 CRC64;
     MRGPVKIVAT VGPSSSSASI LAQMLSLGVD VARINASHGG VEQWNSMLES LRRAEEAVGK
     RVGVAVDLEG PRVRTGNSEP VKLEKGDLVT LGFMEGDVPV DARQFFETID EGDIVLLDDG
     KIILQVESVE GFRVKARVLE GGVLGPRKGV VVRGKEPDLP PLSAKDRRAL EFFADKGVSH
     VYVSFARSAE HVEKVRTVVR RLGLRQARIF AKIEGPSGVS RIGEIAEASD GVIIARGDLG
     MHYSLEELPE IQELIVWEAR KRYKTVVLAT EFLSSMIEKP VPTRSEVVDI YQAVLQTADA
     LMLTGETAIG KYPVKSVQWM AKISSRAYKK LATSPPERPR PTSTPYKLAL GLVELAESLD
     SPLVVYSKTG RFAERLASFK PLKTFYVGVP SREVERVVRH LWGAEPIVVG DYPYEAGLAK
     TYEKLRRENI IHGDETVVEA AWSSERGIYI IRVRNLEF
//