ID   PCKG_CHLTE              Reviewed;         621 AA.
AC   Q8KAD1;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
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}; Synonyms=pckA;
GN   OrderedLocusNames=CT2232;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM73448.1; -; Genomic_DNA.
DR   RefSeq; NP_663106.1; NC_002932.3.
DR   RefSeq; WP_010933885.1; NC_002932.3.
DR   AlphaFoldDB; Q8KAD1; -.
DR   SMR; Q8KAD1; -.
DR   STRING; 194439.CT2232; -.
DR   PRIDE; Q8KAD1; -.
DR   EnsemblBacteria; AAM73448; AAM73448; CT2232.
DR   KEGG; cte:CT2232; -.
DR   PATRIC; fig|194439.7.peg.2025; -.
DR   eggNOG; COG1274; Bacteria.
DR   HOGENOM; CLU_028872_1_1_10; -.
DR   OMA; GPTNNWV; -.
DR   OrthoDB; 267285at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001007; 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..621
FT                   /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT                   /id="PRO_0000103599"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         218..220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         227
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         247
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         270..275
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         296
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         386..388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         388
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         419
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
FT   BINDING         512..515
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
SQ   SEQUENCE   621 AA;  69933 MW;  5F07BF2C8DA4C003 CRC64;
     MEPIPINAPD SVRNLKLLQW VRETAELCQP DSVCWCDGSV EEYDRLCNEM VASGTFIKLS
     EQKRPNSYLC RSDPSDVARV EDRTFICSIR RQDAGPTNNW VAPKEMKATL NKLLAGCMKG
     RTMYIIPFSM GPLGSHIAHI GVEITDSPYV VTNMRIMTRM GRAVLDLLDE EAEFVPCLHS
     VGAPLEPGQQ DVPWPCNDTK YIVHFPEERS IVSYGSGYGG NALLGKKCFA LRIASSMARD
     EGWLAEHMLI LGVESPEGEK DYVAAAFPSA CGKTNFAMMI PPGEMEGWKI TTVGDDIAWI
     KQGKDGRLYA INPEYGFFGV APGTSEKSNP NAMATLHANC IFTNVALTPD GDVWWEGMTD
     TPPDFLIDWQ GKPWVPGCER PAAHPNARFT APAHQCPVID ENWENPDGVP ISAFIFGGRR
     GDTIPLVYQS ANWYYGVYLA ATMGSEKTAA AAGKIGDVRR DPFAMLPFCG YHMGDYFNHW
     LHVGRTLTDP PRIFGVNWFR KDENGKFLWP GFGENMRVLK WIIGRVHGRA AAVESPLGWM
     PRYESLDWRG LDGFTRDKFS TLMSVDREAW KQELFSHEEL LEKLYDRLPK EFTHIRELML
     STLWRSPEHW ELAPERYTAE H