KPYK_PYRAE
ID KPYK_PYRAE Reviewed; 461 AA.
AC Q8ZYE0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pyk; OrderedLocusNames=PAE0819;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
RN [2]
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, AND REGULATION.
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
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=46 umol/min/mg enzyme (at 65 degrees Celsius)
CC {ECO:0000269|PubMed:12654928};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:12654928};
CC Temperature dependence:
CC Optimum temperature is higher than 98 degrees Celsius. Thermostable
CC for 2 hours up to 100 degrees Celsius. {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; AE009441; AAL63053.1; -; Genomic_DNA.
DR PDB; 3QTG; X-ray; 2.20 A; A/B=1-461.
DR PDBsum; 3QTG; -.
DR AlphaFoldDB; Q8ZYE0; -.
DR SMR; Q8ZYE0; -.
DR STRING; 178306.PAE0819; -.
DR EnsemblBacteria; AAL63053; AAL63053; PAE0819.
DR KEGG; pai:PAE0819; -.
DR PATRIC; fig|178306.9.peg.602; -.
DR eggNOG; arCOG04120; Archaea.
DR HOGENOM; CLU_015439_1_1_2; -.
DR InParanoid; Q8ZYE0; -.
DR OMA; QVPIVQK; -.
DR BRENDA; 2.7.1.40; 5239.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..461
FT /note="Pyruvate kinase"
FT /id="PRO_0000295181"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 48..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 48
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 230
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:3QTG"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 208..220
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:3QTG"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3QTG"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 358..373
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 385..391
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:3QTG"
FT HELIX 428..439
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:3QTG"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:3QTG"
SQ SEQUENCE 461 AA; 50262 MW; D43333DA69BDE14C CRC64;
MSAPRGDHAI LRARNLTKRV ATLGPSTDVL RPDELIKFLD LVDGVRINLA HASPNEVKFR
IEAVRSYEKA KNRPLAVIVD LKGPSIRVGS TSPINVQEGE VVKFKLSDKS DGTYIPVPNK
AFFSAVEQND VILMLDGRLR LKVTNTGSDW IEAVAESSGV ITGGKAIVVE GKDYDISTPA
EEDVEALKAI SPIRDNIDYV AISLAKSCKD VDSVRSLLTE LGFQSQVAVK IETKGAVNNL
EELVQCSDYV VVARGDLGLH YGLDALPIVQ RRIVHTSLKY GKPIAVATQL LDSMQSSPIP
TRAEINDVFT TASMGVDSLW LTNETASGKY PLAAVSWLSR ILMNVEYQIP QSPLLQNSRD
RFAKGLVELA QDLGANILVF SMSGTLARRI AKFRPRGVVY VGTPNVRVAR SLSIVWALEP
LYIPAENYEE GLEKLISLKG TTPFVATYGI RGGVHSVKVK L
