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Database: UniProt/TrEMBL
Entry: B3E262_GEOLS
LinkDB: B3E262_GEOLS
Original site: B3E262_GEOLS 
ID   B3E262_GEOLS            Unreviewed;       616 AA.
AC   B3E262;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   19-FEB-2014, entry version 38.
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=Glov_3462;
OS   Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=398767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1151 / DSM 17278 / SZ;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L.,
RA   Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y.,
RA   Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.;
RT   "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL   Submitted (MAY-2008) 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   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family.
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DR   EMBL; CP001089; ACD97165.1; -; Genomic_DNA.
DR   RefSeq; YP_001953685.1; NC_010814.1.
DR   STRING; 398767.Glov_3462; -.
DR   EnsemblBacteria; ACD97165; ACD97165; Glov_3462.
DR   GeneID; 6368947; -.
DR   KEGG; glo:Glov_3462; -.
DR   PATRIC; 21998591; VBIGeoLov31523_3384.
DR   eggNOG; COG1274; -.
DR   HOGENOM; HOG000191700; -.
DR   KO; K01596; -.
DR   OMA; WMRFGED; -.
DR   OrthoDB; EOG6MPWQS; -.
DR   ProtClustDB; PRK04210; -.
DR   BioCyc; GLOV398767:GH32-3514-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; 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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Decarboxylase; Gluconeogenesis;
KW   GTP-binding; Kinase; Lyase; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyruvate; Transferase.
FT   NP_BIND     262    267       GTP (By similarity).
FT   NP_BIND     506    509       GTP (By similarity).
FT   REGION      380    382       Substrate binding (By similarity).
FT   ACT_SITE    263    263       By similarity.
FT   METAL       219    219       Manganese (By similarity).
FT   METAL       239    239       Manganese; via tele nitrogen (By
FT                                similarity).
FT   METAL       290    290       Manganese (By similarity).
FT   BINDING      72     72       Substrate (By similarity).
FT   BINDING     212    212       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     219    219       Substrate (By similarity).
FT   BINDING     261    261       Substrate (By similarity).
FT   BINDING     382    382       GTP (By similarity).
FT   BINDING     413    413       GTP (By similarity).
SQ   SEQUENCE   616 AA;  69354 MW;  63C63D9F8456221F CRC64;
     MSYEVKNEQL KAWVAEVEAM CEPANIHWCD GSQEEYDRLC GQMVESGTFR KLNPEKRPNS
     YLAFSDPIDV ARVEDRTFIC SLNKQDAGPT NNWVAPKEMK ETLKGLFKGC MKGRTMYVIP
     FSMGPLGSNI AKIGVEITDS PYVVVNMRIM TRMGKQVLDV LGNGEFVPCL HSVGMPLAEG
     QKDVAWPCNK EKYIVHFPEE RAIWSFGSGY GGNALLGKKC LALRIASVQA RDEGWLAEHM
     LILGVESPTG EKSYVGAAFP SACGKTNFAM LIPPKPFQDK GWKVTTIGDD IAWIKPGADG
     QVYAINPEYG YFGVAPGTNY KTNPNAMISC EKNSIFTNVA LTEDGDVWWE GMDGEVPAKL
     TDWQGNAWTP DCGRPAAHPN ARFTAPASQC PCIDPEWENP KGVPMSAFIF GGRRKDTVPL
     VYQAFNWNYG VYLASTLGSE TTAAAVGATG NVRRDPFAML PFCGYHMADY FAHWLQFGRS
     IARPPRIFSV NWFRKDANGK FIWPGYGENM RVLKWIAERV QGKTGSVECP LGWMPRYEDM
     DWEGIEMSRE KFNELMSVDR DVWQNEVISH EELFVKMYDK LPKEFLHIRE LILSSLWRSP
     EHWEQIGEVH PEGWNE
//
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