PCKG_CHLLI
ID PCKG_CHLLI Reviewed; 618 AA.
AC Q08262;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 103.
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;
OS Chlorobium limicola.
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=1092;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8448205; DOI=10.1016/0167-4781(93)90213-w;
RA Xie D.L., Lill H., Hauska G., Maeda M., Futai M., Nelson N.;
RT "The atp2 operon of the green bacterium Chlorobium limicola.";
RL Biochim. Biophys. Acta 1172:267-273(1993).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB25776.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; S56812; AAB25776.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q08262; -.
DR SMR; Q08262; -.
DR UniPathway; UPA00138; -.
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.
FT CHAIN 1..618
FT /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT /id="PRO_0000103595"
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 510..513
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00452"
SQ SEQUENCE 618 AA; 69531 MW; 274A1FA8D0612C29 CRC64;
MEPIPINAPD YVKNLKLLQW VKETVALCQP DSVCWCDGST EEYDRLCEEM VNSGTFIKLS
EQKRPNSYLC RSDPSDVARV EDRTFICSIR RQDAGPTNNW VAPKEMKATL NKLFTGCMKG
RTMYVIPFSM GPLGSHIAHI GVEITDSPYV VTNMRIMTRM GRQVLELLDE EAEFVPCLHS
VGAPLEPGQA DVPWPCNDTK YIVHFPEEHA IVSYSSGYNG NTLLGKKCFA LRIASSMARD
EGWLAEHMLI LGVESPAGEK DYVAAAFPSA CGKTNFAMII PPGEMEGWKI TTVGDDIRLD
QQGKDGRLHA INPEYGFFGV APGTSDKSNP NAMATLHANC IFTNVALTPD GDVWWEDMTD
TPPEYLIDWQ GKPWVPGCDR PAAHPNSRFT APASQCPVID PAWENPRVLP ISAFIFAGRR
GDTIPLVYQS SNWYYGVYMA ATMGSEKTAA AARSATCVDP FAMLPFCGYH MGDYFNHWLH
VGRTVSDPPR IFIVNWFRKT RTGKFLWPGF GDNMRVLKWM MGRVHGRSGA VESPLGWMPR
YESLDWRGLD GFTSNKFSKL MSVDREGKQE LFSHEELLEK LYDRLPKEFT HIRELLLSTL
WMSPEHWELA PELYSAES
