KPYK_AERPE
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 03-AUG-2022, entry version 114.
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; Crenarchaeota; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 OMA; QVPIVQK; -.
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 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; IPR015793; Pyrv_Knase_brl.
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 PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 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
