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Database: UniProt
Entry: Q6F494
LinkDB: Q6F494
Original site: Q6F494 
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   14-MAY-2014, entry version 74.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP];
DE            Short=PEP carboxykinase;
DE            Short=PEPCK;
DE            EC=4.1.1.32;
DE   AltName: Full=PckTk;
GN   Name=pckG; Synonyms=pck; OrderedLocusNames=TK1405;
OS   Thermococcus kodakaraensis (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,
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; IACNIGR; -.
DR   BioCyc; TKOD69014:GH72-1426-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-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; SSF68923; 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; via tele nitrogen (By
FT                                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
//
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