ID   PCKG_NEOFR              Reviewed;         608 AA.
AC   P22130;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP];
DE            Short=PEPCK;
DE            EC=4.1.1.32;
OS   Neocallimastix frontalis (Rumen fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=4757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1339359; DOI=10.1016/0378-1119(92)90444-t;
RA   Reymond P., Geourjon C., Roux B., Durand R., Fevre M.;
RT   "Sequence of the phosphoenolpyruvate carboxykinase-encoding cDNA from the
RT   rumen anaerobic fungus Neocallimastix frontalis: comparison of the amino
RT   acid sequence with animals and yeast.";
RL   Gene 110:57-63(1992).
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:0000250}.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family. {ECO:0000305}.
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DR   EMBL; M59372; AAA33553.1; -; mRNA.
DR   PIR; JQ1462; JQ1462.
DR   AlphaFoldDB; P22130; -.
DR   SMR; P22130; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese;
KW   Metal-binding; Nucleotide-binding.
FT   CHAIN           1..608
FT                   /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT                   /id="PRO_0000103636"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         215..217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         224
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         268..273
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         292
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         386..388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         388
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         419
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         513..516
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
SQ   SEQUENCE   608 AA;  66904 MW;  C4D2B249A92B7D26 CRC64;
     MAHSVSSVVN KQLLAYIKES SELMTPKDIY VCDGSAEEYH NLCELLVKQG IFTKLNETKR
     PNCYLARSNP ADVARVEKCT YICSEKEEDA GPTNNWMAPA EMKAKLNGLM KGCMKGRTMY
     VIPFSMGPIG GPISRVGVEI TDSPYVVVNM CIMAKVGKKV LDLLGVDGTF VPCTHSCLAP
     LEEGQKDSTW PCNIDNRYIV QFPEEHRIVS VGSGYGGNAL LGKKCYALRI ATVLSREAGD
     SLAEHMLILG ITNPQGKKYY ITAAFPSACG KTNLAMLNAT IPGWKIECVG DDIAWLKIGK
     DGRLWAINPE SGFFGVAPGT SYKSNPNAMK SCEKDTIFTN VALTEDGDVW WEGMTKEVPK
     GKIITWLGKE WSADSGEPKP NLAHPNSRFT ARVENVPVGD PGYYALEGVP VSAMIFGGRR
     ENTVPLVFQS RSWKHGVLLG SSVASETTAA AEAAAGQLRF DPFAMLPFCG YNMGDYFGYW
     LSFADKYDEA KLPKIFHVNW FRKDNGRFLW PGYGENSRVL KWIIERVEGK EGIAKETPIG
     YLPAKGALDL SGLDVPEADM EKILTVDCKA YLSEVEKIRQ YHSKFGSLLP KALIAELDAL
     EQRLKAAL