ID   PCKG_FRASC              Reviewed;         609 AA.
AC   Q2J645;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=Francci3_3897;
OS   Frankia sp. (strain CcI3).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CP000249; ABD13247.1; -; Genomic_DNA.
DR   RefSeq; YP_482976.1; -.
DR   GeneID; 3906665; -.
DR   GenomeReviews; CP000249_GR; Francci3_3897.
DR   KEGG; fra:Francci3_3897; -.
DR   HOGENOM; Q2J645; -.
DR   OMA; Q2J645; SHPNARF.
DR   BioCyc; FSP106370:FRANCCI3_3897-MON; -.
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:UniProtKB-KW.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) act...; IEA:HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:HAMAP.
DR   HAMAP; MF_00452; -; 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   Gene3D; G3DSA:3.90.228.20; PEP_carboxykinase_C; 1.
DR   Gene3D; G3DSA:3.40.449.10; PEP_carboxykinase_N; 1.
DR   PANTHER; PTHR11561; PEP_carboxykin; 1.
DR   Pfam; PF00821; PEPCK; 1.
DR   PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR   ProDom; PD004738; PEPCK_N; 1.
DR   PROSITE; PS00505; PEPCK_GTP; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Decarboxylase; Gluconeogenesis;
KW   GTP-binding; Lyase; Manganese; Metal-binding; Nucleotide-binding.
FT   CHAIN         1    609       Phosphoenolpyruvate carboxykinase [GTP].
FT                                /FTId=PRO_1000060290.
FT   NP_BIND     273    278       GTP (By similarity).
FT   NP_BIND     515    518       GTP (By similarity).
FT   REGION      387    389       Substrate binding (By similarity).
FT   ACT_SITE    274    274       By similarity.
FT   METAL       230    230       Manganese (By similarity).
FT   METAL       250    250       Manganese (By similarity).
FT   METAL       297    297       Manganese (By similarity).
FT   BINDING      82     82       Substrate (By similarity).
FT   BINDING     223    223       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     230    230       Substrate (By similarity).
FT   BINDING     272    272       Substrate (By similarity).
FT   BINDING     389    389       GTP (By similarity).
FT   BINDING     420    420       GTP (By similarity).
SQ   SEQUENCE   609 AA;  66912 MW;  3790D69E45471916 CRC64;
     MTTAAQVSGL DVAPTRHARL VAWVREIAEL TQPDRVEWCD GSEAEFDRLT SLLIEQGTLV
     RLNDEKRPNS FYAASDPGDV ARVEDRTYIC SEQAEDAGPT NNWLDPAEMR ATLRGLFAGC
     MRGRTMYVVP FCMGPLGSRI SALGVEITDS PYVVISMRTM TRMGTPALEQ LGTDGFFVPA
     VHSLGAPLEP GQADVPWPCN TTKYITHFPE TREIWSYGSG YGGNALLGKK CYALRIASVM
     ARDEGWLAEH MLILKLTSPA GKVHYIAAAF PSACGKTNLA MLIPTLPGWQ AETVGDDIAW
     MRFGEDGRLY AVNPEAGFFG VAPGTGEQTN PNAVRTLWGN AIYTNVARTD NGDVWWEGLT
     KQPPAHLIDW KGRDWTPESS EPAAHPNARF TVPAGQCPTI APEWEDPRGV PISAILFGGR
     RATAVPLVTE APDWRRGVFF GSIVASETTA AQAGAIGKLR RDPFAMLPFC GYNMADYFAH
     WLEVGQKADQ TKLPRVYYVN WFRKSPEGRF LWPGFGDNSR VLAWIVGRLE GTAAGVETPL
     GVLPTKDALP VDGIDIAEED LETLLTVDVE VWKQEAQLIP EHYQTFGERL PAALWTEHEA
     LVERLNSAD
//