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Database: UniProt/TrEMBL
Entry: E8RA45_DESM0
LinkDB: E8RA45_DESM0
Original site: E8RA45_DESM0 
ID   E8RA45_DESM0            Unreviewed;       629 AA.
AC   E8RA45;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   19-FEB-2014, entry version 20.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP];
DE            Short=PEP carboxykinase;
DE            Short=PEPCK;
DE            EC=4.1.1.32;
DE   AltName: Full=Phosphoenolpyruvate carboxylase;
GN   Name=pckG; OrderedLocusNames=Desmu_0004;
OS   Desulfurococcus mucosus (strain ATCC 35584 / DSM 2162 / JCM 9187 /
OS   O7/1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Desulfurococcus.
OX   NCBI_TaxID=765177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35584 / DSM 2162 / JCM 9187 / O7/1;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA   Chertkov O., Held B., Brettin T., Detter J.C., Tapia R., Han C.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Wirth R., Bilek Y., Hader T., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Desulfurococcus mucosus DSM 2162.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: GTP + oxaloacetate = GDP + phosphoenolpyruvate
CC       + CO(2).
CC   -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family.
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DR   EMBL; CP002363; ADV64323.1; -; Genomic_DNA.
DR   RefSeq; YP_004175805.1; NC_014961.1.
DR   EnsemblBacteria; ADV64323; ADV64323; Desmu_0004.
DR   GeneID; 10152681; -.
DR   KEGG; dmu:Desmu_0004; -.
DR   HOGENOM; HOG000191700; -.
DR   KO; K01596; -.
DR   OMA; WMRFGED; -.
DR   BioCyc; DMUC765177:GHQE-4-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:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Decarboxylase; Gluconeogenesis;
KW   GTP-binding; Kinase; Lyase; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyruvate; Transferase.
FT   REGION      390    392       Substrate binding (By similarity).
FT   ACT_SITE    278    278       By similarity.
FT   METAL       235    235       Manganese (By similarity).
FT   METAL       254    254       Manganese; via tele nitrogen (By
FT                                similarity).
FT   METAL       294    294       Manganese (By similarity).
FT   BINDING      92     92       Substrate (By similarity).
FT   BINDING     228    228       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     235    235       Substrate (By similarity).
FT   BINDING     392    392       GTP (By similarity).
FT   BINDING     423    423       GTP (By similarity).
SQ   SEQUENCE   629 AA;  71760 MW;  A6F7264A09719A7B CRC64;
     MDASVTGLLT RLSRYADERA VERLSRISDR RLLEWITEVV ELLEPASVFV NTGSREDLEY
     IRMRAVEKRE EIPSRYNPRH TVHFDGIYDL ARDRENTRIL TPGGSPIPMV NTGNRDEGLR
     ELREIYRGIM RGKEMYIGFY CFGPRGSPFT LYGVQVTDSA YVMHSENILY RVCYDVFVEK
     GGSMRYMRFL HSAGELNEYG WSRNISKRRI YIDTVDNITY SVNTQYAGNT VGLKKLSLRL
     CVNQGYRENW LCEHMFIVGV KGTGDTISYF TGAFPAGCGK TSTALIADTV VGDDLAMIRN
     VNGEARAVNP EIGMFGIIDG VNPVDDPEIY GILSSRETEV IFSNVLLTED GEVWWNGKPS
     EPRRGVNYAG EWWPGKLDEK GRPIPPSHPN ARFTTSIFYL SKVDPRINDP NGVPVSGMIF
     GGRDSDTWVP VEEAFNWVHG IVTKGASLES ERTTAVLGKA GEREFNPFAI LDFLSVSPGE
     FIELHFRFGD GLEKQPRIYG VNYFLRDEAG RYLTEKVDKR VWLKWMALRV NNEVDALETP
     TGLIPVYEDL AVLFKRELGK EFSIELYEKL FTVRVGKHLE KAERILRIYE NIPGTPRLFF
     DTLIEQKRRL KHALDKYGMF ISPLSLDKR
//
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