ID   PCKG_HAECO              Reviewed;         619 AA.
AC   P29190;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP];
DE            Short=PEPCK;
DE            EC=4.1.1.32;
GN   Name=PEPCK;
OS   Haemonchus contortus (Barber pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Haemonchidae; Haemonchus.
OX   NCBI_TaxID=6289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1741016; DOI=10.1016/0166-6851(92)90226-a;
RA   Klein R.D., Winterrowd C.A., Hatzenbuhler N.T., Shea M.H., Favreau M.A.,
RA   Nulf S.C., Geary T.G.;
RT   "Cloning of a cDNA encoding phosphoenolpyruvate carboxykinase from
RT   Haemonchus contortus.";
RL   Mol. Biochem. Parasitol. 50:285-294(1992).
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; M76494; AAA29180.1; -; mRNA.
DR   PIR; A45625; A45625.
DR   AlphaFoldDB; P29190; -.
DR   SMR; P29190; -.
DR   PRIDE; P29190; -.
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..619
FT                   /note="Phosphoenolpyruvate carboxykinase [GTP]"
FT                   /id="PRO_0000103633"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         230..232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         239
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         259
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         282..287
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         306
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         399..401
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         401
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         432
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
FT   BINDING         525..528
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P07379"
SQ   SEQUENCE   619 AA;  69656 MW;  40A801A1EB647CFD CRC64;
     MKRLGHVPIH KGDFHLLPPK VQRFVAEKAE LMRPRGIYIC DGSQHEADEI IDKLIERGML
     SPLKAYENNY ICRTDPKDVA RVESKTWMVT PDKYQTVCHT PDGIEPIMGH WMSPDSLATE
     LDSRFPGCMA GRIMYVIPFS MGPVGGPLSK IGVQLTDSNY VVLSMRIMTR VGHEVWDALG
     DNDFVRCIHS VGLPRPVKQR VINHWPCNPE RVLIAHRPAE REIWSFGSGY GGNSLLGKKM
     LALRIASNIA KDEGWMAEHM LIMGVTRPDG KEHFIAAAFP SACGKTNLAM LEPALPGWKV
     RCVGDDIAWM KFGEDGRLYA INPEYGFFGV APGTSKKTNP MAVATFQKNS IFTNVGETAN
     GEYFWEGLED EIKDKNVDMI NWLGEKWRIG DPGLCAHPNS RFAAPASQCP IIHPEWESPK
     GVPIDAIIFG GRRPAGVPLV FETRSWLHGI FTGACLKSEA TAAAEHKGKT VMHDPMAMRP
     FMGYNFGHYL QHWIDLNKDG RKVPKIYHVN WFRRDANNKF LWPGYGQNIR VIDWIVRRLD
     GEPDIGVDTP IGIVPKKGAI NASGLPDIQW DELMSVPKEY WTNDAKEIRK FLEEQVGPDL
     PKEIRAEMDA QEERINKQA