ID   PCKG_ANADE              Reviewed;         596 AA.
AC   Q2IFT1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-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=Adeh_3676;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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.
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; CP000251; ABC83442.1; -; Genomic_DNA.
DR   RefSeq; YP_466879.1; -.
DR   GeneID; 3886451; -.
DR   GenomeReviews; CP000251_GR; Adeh_3676.
DR   KEGG; ade:Adeh_3676; -.
DR   HOGENOM; Q2IFT1; -.
DR   OMA; Q2IFT1; SHPNARF.
DR   BioCyc; ADEH290397:ADEH_3676-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    596       Phosphoenolpyruvate carboxykinase [GTP].
FT                                /FTId=PRO_1000060286.
FT   NP_BIND     257    262       GTP (By similarity).
FT   NP_BIND     499    502       GTP (By similarity).
FT   REGION      373    375       Substrate binding (By similarity).
FT   ACT_SITE    258    258       By similarity.
FT   METAL       214    214       Manganese (By similarity).
FT   METAL       234    234       Manganese (By similarity).
FT   METAL       283    283       Manganese (By similarity).
FT   BINDING      77     77       Substrate (By similarity).
FT   BINDING     207    207       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     214    214       Substrate (By similarity).
FT   BINDING     256    256       Substrate (By similarity).
FT   BINDING     375    375       GTP (By similarity).
FT   BINDING     406    406       GTP (By similarity).
SQ   SEQUENCE   596 AA;  65789 MW;  E868169319469F89 CRC64;
     MSTSPAARPT SNPHLLGWVD EMAKLCKPDR VHWCDGSEAE KKRLTDDAVA AKVLIPLDQQ
     KWPGCHYHHS NPSDVARVEH LTFICTPTKE QAGPTNNWME PKEAYRKLGA IFDGSMKGRT
     MYVVPYVMGP STSPFAKVGI EITDSVYVAL NMGIMARMGK VALDRLGDSN EFNRGLHSVA
     DCNPERRFIC HFPQDNTIWS VGSGYGGNAL LGKKCLALRI ASYLAKNEGW LAEHMLILEA
     ESPTGEKQYV AAAFPSACGK TNFAMMIPPA AFPGWKIRTV GDDISWMRVG EDGRLWAVNP
     ENGYFGVAPG TNRKTNPNAM DSVRKDTIFT NVARTPDGDI WWEGMDHEAP AELIDWKGQP
     WKKGSTEKAA HPNSRFTAPA KNNPAISPLV DDPKGVPISA IIFGGRRSTT VPLVLEAFNW
     THGVYLGSTM GSETTAAATG QVGVVRRDPM AMLPFIGYDC GSYLQHWLDM QSRIPNPPKI
     FLVNWFRKSA EGKFLWPGYG DNMRVLKWML DRAAGRAPAK ETLLGYTPGD AGLDLHGLDV
     SKDAIAAATR IDLGEWEQEL ESQAEWFEKL GKTLPAPLAL QRELLLERVR AARKVK
//