PCKGM_DICDI
ID PCKGM_DICDI Reviewed; 653 AA.
AC Q869Z4; Q55AF8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP], mitochondrial;
DE Short=PEPCK-M;
DE EC=4.1.1.32;
DE Flags: Precursor;
GN Name=pck2; ORFNames=DDB_G0271904;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- MISCELLANEOUS: In eukaryotes there are two isozymes: a cytoplasmic one
CC and a mitochondrial one.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000007; EAL71476.1; -; Genomic_DNA.
DR RefSeq; XP_645396.1; XM_640304.1.
DR AlphaFoldDB; Q869Z4; -.
DR SMR; Q869Z4; -.
DR STRING; 44689.DDB0230145; -.
DR PaxDb; Q869Z4; -.
DR EnsemblProtists; EAL71476; EAL71476; DDB_G0271904.
DR GeneID; 8618224; -.
DR KEGG; ddi:DDB_G0271904; -.
DR dictyBase; DDB_G0271904; -.
DR eggNOG; KOG3749; Eukaryota.
DR HOGENOM; CLU_028872_1_1_1; -.
DR InParanoid; Q869Z4; -.
DR OMA; GPTNNWV; -.
DR PhylomeDB; Q869Z4; -.
DR Reactome; R-DDI-70263; Gluconeogenesis.
DR UniPathway; UPA00138; -.
DR PRO; PR:Q869Z4; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IBA:GO_Central.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0046327; P:glycerol biosynthetic process from pyruvate; IBA:GO_Central.
DR GO; GO:0019543; P:propionate catabolic process; IBA:GO_Central.
DR GO; GO:0033993; P:response to lipid; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
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 Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..51
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 52..653
FT /note="Phosphoenolpyruvate carboxykinase [GTP],
FT mitochondrial"
FT /id="PRO_0000328603"
FT ACT_SITE 310
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 257..259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 286
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 309..314
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 333
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 424..426
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 426
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
FT BINDING 555..558
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P07379"
SQ SEQUENCE 653 AA; 72462 MW; BDE051CA1E245333 CRC64;
MLKNFIQKGK LINSISSSSS FQSSTFLNNN GFNSGAWVGS RFFSLEQLKK KTKNQKLINW
VEEQAKLCKP DNIYICDGSE EEFKKFTDDM VKSGTLIKLN SKRPNSFLAR SDPSDVARVE
SRTYICAKTK EDAGPTNNWM DPNQMKQTLK PLFNGSMKGR TMYVMPFSMG PLGSDISHIG
VQVTDSPFVV CNMKIMTRMG DKVLNQIKEN DDFVPCLHSV GAPLAKGQKD SHWPCNPNKY
IVHYPEERSI QSFGSGYGGN ALLGKKCFSL RIASSMAKEG GWLAEHMLIL SLTNDKGEKK
YIAAAFPSAC GKTNLAMANS VLPGYKVQVC GDDIAWMTMR NGQLYAINPE FGFFGVAPGT
SASSNPNALA AISKNTLFTN VALTPDNDVW WEGLSSPPPT AIDWLGNEWH PNGEGNNTFA
AHPNSRFTAP LSQCPSIDPE WNNPTGVPIS AVIFGGRRSS TVPLVYQALN WKHGVFMGAS
TASELTAAAE GTVGTLRHDP FAMLPFCGYN MGDYFAHWLS MEQKAGSNAD KLPKIFYVNW
FRKNKTSGKF LWPGFGENVR VLKWIFDRCN STLDTTDGKA TQTPIGFVPS NNSIDLNGLE
INKSSLKELF SLNKSEWLHD LKSMRQFCQQ FGDRLPNEIK NQMDQLENRL NKD
