ID   PCKG_FRAAA              Reviewed;         607 AA.
AC   Q0RCJ7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=FRAAL6204;
OS   Frankia alni (strain ACN14a).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CT573213; CAJ64827.1; -; Genomic_DNA.
DR   RefSeq; YP_716342.1; -.
DR   GeneID; 4233718; -.
DR   GenomeReviews; CT573213_GR; FRAAL6204.
DR   KEGG; fal:FRAAL6204; -.
DR   OMA; Q0RCJ7; SHPNARF.
DR   BioCyc; FALN326424:FRAAL6204-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    607       Phosphoenolpyruvate carboxykinase [GTP].
FT                                /FTId=PRO_1000060289.
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   607 AA;  66582 MW;  01D266786EDFF796 CRC64;
     MTTAAQIPGL EAAPTKHARL VAWVREIAEL TQPERVEWCD GSEAEFDRLT SLLIEKGTLV
     RLNDEKRPNS FYAASDPSDV ARVEDRTYIC SEKAEDAGPT NNWMDPAEMR VKLQGLFEGS
     MRGRTMYVVP FCMGPLGSHI SALGVEITDS PYVVISMRTM TRMGAPALEQ LGEDGFFVPA
     VHSLGAPLES GAADVPWPCN TTKYITHFPE TREIWSYGSG YGGNALLGKK CYALRIASVM
     ARDEGWLAEH MLILKLTSPA GKVHYIAAAF PSACGKTNLA MLIPTLPGWK AETVGDDIAW
     MRFGEDGRLY AVNPEAGFFG VAPGTGEQTN PNAIKTLWGN TVFTNVARTD DGDVWWEGLT
     KQAPGHLTDW KGRDWTPEST EPAAHPNARF TVPAGQCPTI ASEWQDPKGV PISAILFGGR
     RATAVPLVTE APDWRRGVFF GSIVASETTA AQAGAIGKLR RDPFAMLPFC GYNMADYFAH
     WLEVGQKADQ AKLPRIYYVN WFRKSPEGKF LWPGFGENSR VLAWIVGRLE GHADGVETPL
     GVLPTRDALP TDGLQIDEAD LDALLTVDID VWKQEAELIP EHYQTFGDRL PAALWAEHEA
     LVSRLDG
//