ID   PCKG_LEIXX              Reviewed;         612 AA.
AC   Q6AGS4;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000255|HAMAP-Rule:MF_00452};
DE            Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00452};
DE            Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00452};
DE            EC=4.1.1.32 {ECO:0000255|HAMAP-Rule:MF_00452};
GN   Name=pckG {ECO:0000255|HAMAP-Rule:MF_00452}; OrderedLocusNames=Lxx04240;
OS   Leifsonia xyli subsp. xyli (strain CTCB07).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia.
OX   NCBI_TaxID=281090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTCB07;
RX   PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827;
RA   Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA   Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA   de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA   Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA   El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA   Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA   Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA   Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA   Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT   "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT   subsp. xyli.";
RL   Mol. Plant Microbe Interact. 17:827-836(2004).
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 derived
CC       from the citric acid cycle. {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00452};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00452};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00452};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00452}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family. {ECO:0000255|HAMAP-Rule:MF_00452}.
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DR   EMBL; AE016822; AAT88421.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6AGS4; -.
DR   SMR; Q6AGS4; -.
DR   STRING; 281090.Lxx04240; -.
DR   EnsemblBacteria; AAT88421; AAT88421; Lxx04240.
DR   KEGG; lxx:Lxx04240; -.
DR   eggNOG; COG1274; Bacteria.
DR   HOGENOM; CLU_028872_1_1_11; -.
DR   OMA; GPTNNWV; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001306; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd00819; PEPCK_GTP; 1.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 1.
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; IPR035077; PEP_carboxykinase_GTP_C.
DR   InterPro; IPR035078; PEP_carboxykinase_GTP_N.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
DR   PANTHER; PTHR11561; PTHR11561; 1.
DR   Pfam; PF00821; PEPCK_GTP; 1.
DR   Pfam; PF17297; PEPCK_N; 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   Cytoplasm; Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..612
FT                   /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT                   /id="PRO_0000103606"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         227..229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         236
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         256
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         279..284
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         303
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         393..395
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         395
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         426
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         520..523
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
SQ   SEQUENCE   612 AA;  66419 MW;  BB6BD41B5049CE6A CRC64;
     MTAPPRPTAP PGAAALTGLA ALHAWVDELA ALLQPDGIVW CDGSRGQTDR LTKQLVAEGK
     LIRLNPEWRP NSFLSRTDPS DVARVEDRTF ICSLDEADAG PTNNWREPEG MRAELREAFA
     GSMRGRTLYV VPFSMGPIGG PLSQLGVQLT DSAYVAVSMG IMTRVASAVL DLIAAGQPWV
     PTVHSVGAPL VDEAGVRQED VAWPCNPVKY IVQFPETREI WSYGSGYGGN AILAKKCFAL
     RIASVMARDE GWLAEHMLIV KVTSPEGRVF HFAAAFPSSC GKTNLAMLKP SIPGWTVETV
     CDDIAWLRPG PDGRLRAINP EAGFFGVAPG TGELTNKTAV EALWGNTIFT NVALRDDGDV
     WWEGLTAEPP AHLIDWEGND WTPASGRPAA HPNSRFTVSA AQCPVIADEW DVVDGVPIDA
     ILFGGRRATN VPLVAQARDW KHGVFIGATI SSEQTAAAEG TVGELRRDPF AMLPFCGYNM
     ADYWAHWLRM GEKLGADAPA IFQVNWFRKG DDGRFLWPGF SENARVIEWI ARRVEGSAGA
     EETAIGRLPL ADELDLDGLG LPAEDLAALF DIDTERWLAE CALTEQYFAR FGPRVPPALT
     AELASLRDKL RA