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Database: UniProt
Entry: Q28CD9_XENTR
LinkDB: Q28CD9_XENTR
Original site: Q28CD9_XENTR 
ID   Q28CD9_XENTR            Unreviewed;       475 AA.
AC   Q28CD9;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase, cytosolic [GTP] {ECO:0000256|ARBA:ARBA00040372};
DE            EC=4.1.1.32 {ECO:0000256|ARBA:ARBA00012306};
DE   AltName: Full=Serine-protein kinase PCK1 {ECO:0000256|ARBA:ARBA00042054};
DE   Flags: Fragment;
GN   Name=pck1 {ECO:0000313|EMBL:CAJ82933.1};
GN   ORFNames=TTpA011c19.1-001 {ECO:0000313|EMBL:CAJ82933.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|EMBL:CAJ82933.1};
RN   [1] {ECO:0000313|EMBL:CAJ82933.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Amaya E., Ashurst J.L., Bonfield J.K., Croning M.D.R., Chen C-K.,
RA   Davies R.M., Francis M.D., Garrett N., Gilchrist M.J., Grafham D.V.,
RA   McLaren S.R., Papalopulu N., Rogers J., Smith J.C., Taylor R.G., Voigt J.,
RA   Zorn A.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + L-seryl-[protein] = GDP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:64020, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:58189, ChEBI:CHEBI:83421;
CC         Evidence={ECO:0000256|ARBA:ARBA00036764};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64021;
CC         Evidence={ECO:0000256|ARBA:ARBA00036764};
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:0000256|ARBA:ARBA00035922};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10389;
CC         Evidence={ECO:0000256|ARBA:ARBA00035922};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10390;
CC         Evidence={ECO:0000256|ARBA:ARBA00035922};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family. {ECO:0000256|ARBA:ARBA00005796}.
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DR   EMBL; CR926436; CAJ82933.1; -; mRNA.
DR   AlphaFoldDB; Q28CD9; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; 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:0043648; P:dicarboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00819; PEPCK_GTP; 1.
DR   Gene3D; 3.90.228.20; -; 1.
DR   Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 1.
DR   Gene3D; 2.170.8.10; Phosphoenolpyruvate Carboxykinase, domain 2; 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; PHOSPHOENOLPYRUVATE CARBOXYKINASE; 1.
DR   PANTHER; PTHR11561:SF19; PHOSPHOENOLPYRUVATE CARBOXYKINASE, CYTOSOLIC [GTP]; 1.
DR   Pfam; PF00821; PEPCK_GTP; 1.
DR   Pfam; PF17297; PEPCK_N; 1.
DR   SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR   SUPFAM; SSF53795; PEP carboxykinase-like; 1.
DR   PROSITE; PS00505; PEPCK_GTP; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAJ82933.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyruvate {ECO:0000313|EMBL:CAJ82933.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..109
FT                   /note="Phosphoenolpyruvate carboxykinase GTP-utilising N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17297"
FT   DOMAIN          113..471
FT                   /note="Phosphoenolpyruvate carboxykinase C-terminal P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF00821"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAJ82933.1"
SQ   SEQUENCE   475 AA;  52978 MW;  B7B6A75FFA0457C5 CRC64;
     GIGSPLSKIG IELTDSPYVV ASMRIMTRMG TAVLETLGDG EFVKCLHSVG CPLPLKKPLV
     NNWPCNPEQT LIAHIPEQRE IISFGSGYGG NSLLGKKCFA LRIASRIAKE EGWLAEHMLI
     LGITNPEGEK KYFAAAFPSA CGKTNLAMMK PSVPGWKIEC VGDDIAWMKF DEHGNLRAIN
     PENGFFGVAP GTSAKTNPYA METIRNNTVF TNVGETSDGG IYWEGINESL DPGVTLTSWK
     NKEWTPEDGE PCAHPNSRFC TPASQCPIID PEWESQEGVP IEGIIFGGRR PTGVPLVYEA
     LNWQHGVFVG SAMRSEATAA AEHKGKVIMH DPFAMRPFFG YNFGKYLAHW LSMEHLPSTK
     MPKIFHVNWF RKDKEGNFLW PGYGENIRVL EWMFKRINGE DCAKETPIGY IPAEGALNLK
     GLGDVNVEEL FELSKEFWED EVKDIKKYLD DQVNADLPYE IERELSALEE RLKQL
//
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