ID PCKG_PYRKO Reviewed; 623 AA.
AC Q6F494;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 01-MAY-2013, entry version 68.
DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP];
DE Short=PEP carboxykinase;
DE Short=PEPCK;
DE EC=4.1.1.32;
DE AltName: Full=PckTk;
DE AltName: Full=Phosphoenolpyruvate carboxylase;
GN Name=pckG; Synonyms=pck; OrderedLocusNames=TK1405;
OS Pyrococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Thermococcus 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,
RP COFACTOR, 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
RT phosphoenolpyruvate carboxykinase from the hyperthermophilic archaeon
RT Thermococcus 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
RT Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus
RT genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to
CC phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC pathway that produces glucose from lactate and other precursors
CC derived from the citric acid cycle.
CC -!- CATALYTIC ACTIVITY: GTP + oxaloacetate = GDP + phosphoenolpyruvate
CC + CO(2).
CC -!- COFACTOR: Binds 1 manganese ion per subunit.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.1 uM for oxaloacetate (at 60 degrees Celsius);
CC KM=131 uM for phosphoenolpyruvate (at 60 degrees Celsius);
CC KM=18.5 uM for GDP (at 60 degrees Celsius);
CC KM=36.1 uM for GTP (at 60 degrees Celsius);
CC Vmax=44.4 umol/min/mg enzyme for the forward reaction (at 60
CC degrees Celsius);
CC Vmax=76.9 umol/min/mg enzyme for the reverse reaction (at 60
CC degrees Celsius);
CC pH dependence:
CC Optimum pH is 7;
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius. Thermostable. Half-
CC life at the optimal temperature is 53 minutes;
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family.
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DR EMBL; AB167819; BAD26729.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD85594.1; -; Genomic_DNA.
DR RefSeq; YP_183818.1; NC_006624.1.
DR ProteinModelPortal; Q6F494; -.
DR STRING; 69014.TK1405; -.
DR EnsemblBacteria; BAD85594; BAD85594; TK1405.
DR GeneID; 3234722; -.
DR KEGG; tko:TK1405; -.
DR eggNOG; COG1274; -.
DR HOGENOM; HOG000191700; -.
DR KO; K01596; -.
DR OMA; WMRFGED; -.
DR ProtClustDB; PRK04210; -.
DR UniPathway; UPA00138; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:HAMAP.
DR GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP.
DR Gene3D; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 2.
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; IPR008210; PEP_carboxykinase_N.
DR PANTHER; PTHR11561; PTHR11561; 1.
DR Pfam; PF00821; PEPCK; 1.
DR PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR SUPFAM; SSF68923; PEP_carboxykinase_N; 1.
DR PROSITE; PS00505; PEPCK_GTP; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Decarboxylase; Gluconeogenesis;
KW GTP-binding; Lyase; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1 623 Phosphoenolpyruvate carboxykinase [GTP].
FT /FTId=PRO_0000103620.
FT REGION 384 386 Substrate binding (By similarity).
FT ACT_SITE 272 272 By similarity.
FT METAL 229 229 Manganese (By similarity).
FT METAL 248 248 Manganese (By similarity).
FT METAL 289 289 Manganese (By similarity).
FT BINDING 86 86 Substrate (By similarity).
FT BINDING 222 222 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 229 229 Substrate (By similarity).
FT BINDING 270 270 Substrate (By similarity).
FT BINDING 386 386 GTP (By similarity).
FT BINDING 418 418 GTP (By similarity).
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
//
