ID   PCKG_ASCSU              Reviewed;         643 AA.
AC   Q05893;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP];
DE            Short=PEPCK;
DE            EC=4.1.1.32;
GN   Name=PEPCK;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Nerve cord, and Pharynx;
RX   PubMed=8375484; DOI=10.1006/expr.1993.1072;
RA   Geary T.G., Winterrowd C.A., Alexander-Bowman S.J., Favreau M.A.,
RA   Nulf S.C., Klein R.D.;
RT   "Ascaris suum: cloning of a cDNA encoding phosphoenolpyruvate
RT   carboxykinase.";
RL   Exp. Parasitol. 77:155-161(1993).
CC   -!- FUNCTION: In parasitic nematodes PEPCK carboxylates phosphoenolpyruvate
CC       to oxaloacetate thus introducing the products of glycolysis to
CC       mitochondrial metabolism.
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   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family. {ECO:0000305}.
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DR   EMBL; L01787; AAA29378.1; -; mRNA.
DR   AlphaFoldDB; Q05893; -.
DR   SMR; Q05893; -.
DR   BioCyc; MetaCyc:MON-18260; -.
DR   SABIO-RK; Q05893; -.
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:InterPro.
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; GTP-binding; Lyase; Manganese; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN           1..643
FT                   /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT                   /id="PRO_0000103632"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         253..255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         262
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         282
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         305..310
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         329
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         422..424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         424
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         455
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         548..551
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
SQ   SEQUENCE   643 AA;  72230 MW;  A9C369959AA79E27 CRC64;
     MRCRSLSHFK DDDFAVVSEV VTHKQNHIPV IKGDFVSLPK HVQRFVAEKA ELMKPSAIFI
     CDGSQNEADE LIARCVERGV LVPLKAYKNN YLCRTDPRDV ARVESKTWMI TPEKYDSVCH
     TPEGVKPMMG QWMSPDEFGK ELDDRFPGCM AGRTMYVIPY SMGPVGGPLS KIGIELTDSD
     YVVLCMRIMT RMGEPVLKAL AKNNGEFVRC VHSVGQPKPV ATKVINHWPC NPEKTIIAHR
     PAEREIWSFG SGYGGNSLLG KKCFALRIAM NIGYDEGWMA EHMLIMGVTS PKGEERFVAA
     AFPSACGKTN LAMLEPTIPG WKVRVIGDDI AWMKFGADGR LYAINPEYGF FGVAPGTSHK
     TNPMAMASFQ ENTIFTNVAE TADGEYFWEG LEHEVKNPKV DMINWLGEPW HIGDESKAAH
     PNSRFTAPAG QCPIIHPDWE KPEGVPIDAI IFGGRRPEGV PLVFESRSWV HGIFVGACVK
     SEATAAAEHT GKQVMHDPMA MRPFMGYNFG RYMRHWMKLG QPPHKVPKIF HVNWFRQSAD
     HKFLWPGYGD NIRVIDWILR RCSGDATIAE ETPIGFIPKK GTINLEGLPN VNWDELMSIP
     KSYWLEDMVE TKTFFENQVG SDLPPEIAKE LEAQTERIKA LKE