PCKG_THEKO
ID PCKG_THEKO Reviewed; 623 AA.
AC Q6F494;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:15231795};
DE Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:15231795};
DE Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:15231795};
DE EC=4.1.1.32 {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000269|PubMed:15231795};
DE AltName: Full=GTP-dependent phosphoenolpyruvate carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:15231795};
DE Short=GTP-PEPCK {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:15231795};
DE AltName: Full=PckTk {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000303|PubMed:15231795};
GN Name=pckG; Synonyms=pck; OrderedLocusNames=TK1405;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15231795; DOI=10.1128/jb.186.14.4620-4627.2004;
RA Fukuda W., Fukui T., Atomi H., Imanaka T.;
RT "First characterization of an archaeal GTP-dependent phosphoenolpyruvate
RT carboxykinase from the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1.";
RL J. Bacteriol. 186:4620-4627(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of
CC oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step
CC in the metabolic pathway that produces glucose from lactate and other
CC precursors derived from the citric acid cycle. {ECO:0000255|HAMAP-
CC Rule:MF_00452, ECO:0000269|PubMed:15231795}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00452,
CC ECO:0000269|PubMed:15231795};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00452,
CC ECO:0000269|PubMed:15231795};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00452,
CC ECO:0000269|PubMed:15231795};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.1 uM for oxaloacetate (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:15231795};
CC KM=131 uM for phosphoenolpyruvate (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:15231795};
CC KM=18.5 uM for GDP (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:15231795};
CC KM=36.1 uM for GTP (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:15231795};
CC Vmax=44.4 umol/min/mg enzyme for the forward reaction (at 60 degrees
CC Celsius) {ECO:0000269|PubMed:15231795};
CC Vmax=76.9 umol/min/mg enzyme for the reverse reaction (at 60 degrees
CC Celsius) {ECO:0000269|PubMed:15231795};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:15231795};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius. Thermostable. Half-life at
CC the optimal temperature is 53 minutes. {ECO:0000269|PubMed:15231795};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15231795}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00452,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000255|HAMAP-Rule:MF_00452, 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; AB167819; BAD26729.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD85594.1; -; Genomic_DNA.
DR RefSeq; WP_011250356.1; NC_006624.1.
DR AlphaFoldDB; Q6F494; -.
DR SMR; Q6F494; -.
DR STRING; 69014.TK1405; -.
DR EnsemblBacteria; BAD85594; BAD85594; TK1405.
DR GeneID; 3234722; -.
DR KEGG; tko:TK1405; -.
DR PATRIC; fig|69014.16.peg.1367; -.
DR eggNOG; arCOG05865; Archaea.
DR HOGENOM; CLU_028872_1_1_2; -.
DR InParanoid; Q6F494; -.
DR OMA; GPTNNWV; -.
DR OrthoDB; 37571at2157; -.
DR PhylomeDB; Q6F494; -.
DR BRENDA; 4.1.1.32; 5246.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IBA:GO_Central.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0046327; P:glycerol biosynthetic process from pyruvate; IBA:GO_Central.
DR GO; GO:0019543; P:propionate catabolic process; IBA:GO_Central.
DR GO; GO:0033993; P:response to lipid; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR CDD; cd00819; PEPCK_GTP; 1.
DR Gene3D; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 1.
DR HAMAP; MF_00452; PEPCK_GTP; 1.
DR InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008209; PEP_carboxykinase_GTP.
DR InterPro; IPR035077; PEP_carboxykinase_GTP_C.
DR InterPro; IPR035078; PEP_carboxykinase_GTP_N.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR PANTHER; PTHR11561; PTHR11561; 1.
DR Pfam; PF00821; PEPCK_GTP; 1.
DR Pfam; PF17297; PEPCK_N; 1.
DR PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR SUPFAM; SSF68923; SSF68923; 1.
DR PROSITE; PS00505; PEPCK_GTP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..623
FT /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT /id="PRO_0000103620"
FT ACT_SITE 272
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 220..222
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 271..276
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 289
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 384..386
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 386
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT BINDING 418
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
SQ SEQUENCE 623 AA; 72039 MW; 91B376391DC8B54E CRC64;
MNALERLEKL LDKEQFEKVK AIDNPELHEF LAEWIEWLEP DKVFVCTDSP EDEGYVRWKA
LYYGEERMLE TPNHTVHYDN YYDQARDKAN TAILLPGGKK LPYINTKDRD EGLKEIRELM
KGIMKGKELF VCFFVLGPKN SIFTIPAVQL TDSAYVAHSE FILYRKGYEE FKRLGRSARF
FRFVHSAGEL DERKTSKNLD KRRIYIDLED ETVYSVNTQY GGNTIGLKKL AFRLTIKRAV
EEGWLSEHMF LMRVNGPHGR KTYFTGAYPS MCGKTSTAMI PWENIVGDDL TFILPVNGIA
RGANVEKGVF GIIQGVNPED DPIIWQVLHS PVEIIFSNVL VKDGKPYWND MGIEIPDEGE
NHSGKWWRGK KDAEGNEIPP SHKNARFTVS LEHFPNVDME ALENPCGVEV GGMIFGGRDA
DTWPPVREAF NWEHGVITMG ASLESETTAA TLGKEGVRAF NPMAILDFMS VHLGDYLRNY
LEFGRKLKKT PKIFAVNYFL RENGVWLNHK LDKAVWLKWM ELRVHGDVEA IETPIGYIPK
YKDLAKLFKD VLNKEYTKED YERQFKIRVP ELLAKIDRIE EIYRKLDNVP EELFKVLEEE
RQRLLEAREK YGDYISPFAL EGE
