PECK1_ENTHI
ID PECK1_ENTHI Reviewed; 1151 AA.
AC C4LY96;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=PPi-type phosphoenolpyruvate carboxykinase 1 {ECO:0000303|PubMed:26269598};
DE Short=EhPEPCK1 {ECO:0000303|PubMed:26269598};
DE Short=PPi-PEPCK1 {ECO:0000303|PubMed:26269598};
DE EC=4.1.1.38 {ECO:0000269|PubMed:26269598};
DE AltName: Full=Diphosphate-dependent phosphoenolpyruvate carboxykinase 1 {ECO:0000305};
DE AltName: Full=PEP carboxyphosphotransferase 1 {ECO:0000305};
GN Name=PEPCK1 {ECO:0000305};
GN ORFNames=EHI_166920 {ECO:0000312|EMBL:EAL49379.1};
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS {ECO:0000312|Proteomes:UP000001926};
RX PubMed=15729342; DOI=10.1038/nature03291;
RA Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA Barrell B.G., Fraser C.M., Hall N.;
RT "The genome of the protist parasite Entamoeba histolytica.";
RL Nature 433:865-868(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=26269598; DOI=10.1074/jbc.m115.672907;
RA Chiba Y., Kamikawa R., Nakada-Tsukui K., Saito-Nakano Y., Nozaki T.;
RT "Discovery of PPi-type phosphoenolpyruvate carboxykinase genes in
RT eukaryotes and bacteria.";
RL J. Biol. Chem. 290:23960-23970(2015).
CC -!- FUNCTION: Inorganic pyrophosphate (PPi)-dependent phosphoenolpyruvate
CC carboxykinase, which regulates the carbon flow of the central
CC metabolism by fixing CO(2) to phosphoenolpyruvate to produce
CC oxaloacetate. Can also produce pyruvate and diphosphate from
CC phosphoenolpyruvate and phosphate. {ECO:0000269|PubMed:26269598}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + oxaloacetate = CO2 + phosphate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:22356, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58702; EC=4.1.1.38;
CC Evidence={ECO:0000269|PubMed:26269598};
CC -!- SUBUNIT: Monomer and trimer; forms heterotrimers with PEPCK2 and
CC PEPCK3. {ECO:0000269|PubMed:26269598}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26269598}.
CC -!- SIMILARITY: Belongs to the PPi-type phosphoenolpyruvate carboxykinase
CC family. {ECO:0000305}.
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DR EMBL; DS571177; EAL49379.1; -; Genomic_DNA.
DR RefSeq; XP_654765.1; XM_649673.1.
DR AlphaFoldDB; C4LY96; -.
DR SMR; C4LY96; -.
DR STRING; 5759.rna_EHI_166920-1; -.
DR EnsemblProtists; rna_EHI_166920-1; rna_EHI_166920-1; EHI_166920.
DR GeneID; 3409079; -.
DR KEGG; ehi:EHI_166920; -.
DR VEuPathDB; AmoebaDB:EHI5A_126350; -.
DR VEuPathDB; AmoebaDB:EHI5A_194890; -.
DR VEuPathDB; AmoebaDB:EHI5A_252600; -.
DR VEuPathDB; AmoebaDB:EHI_166920; -.
DR VEuPathDB; AmoebaDB:KM1_081510; -.
DR VEuPathDB; AmoebaDB:KM1_309960; -.
DR eggNOG; ENOG502QW6Z; Eukaryota.
DR HOGENOM; CLU_275663_0_0_1; -.
DR InParanoid; C4LY96; -.
DR OMA; CVILAPH; -.
DR BRENDA; 4.1.1.38; 2080.
DR Proteomes; UP000001926; Partially assembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030585; F:phosphoenolpyruvate carboxykinase (diphosphate) activity; IDA:UniProtKB.
DR GO; GO:0070208; P:protein heterotrimerization; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Decarboxylase; Lyase; Reference proteome.
FT CHAIN 1..1151
FT /note="PPi-type phosphoenolpyruvate carboxykinase 1"
FT /id="PRO_0000434730"
FT COILED 1083..1129
FT /evidence="ECO:0000255"
SQ SEQUENCE 1151 AA; 130909 MW; 2B4806BFD2355379 CRC64;
MFNQEKGTDY PILNIQELEA LADLKLSAMG KEYPKHDKSD AIDVVAPLVD IIAEGDQEST
APIDARLQTF LNSYFAECGE EVPKIPDNTF ILDREGLGRV LSFPPHKQEF FCETMKSYKI
KQGVLHNPAK DKRTTVGVFH ICQSDVPVPA DKIECPKIAF LRMLKAAFYG APDDHLIIPY
TAECKEPTRS WVSLYMRPVV VPGVKGVKGF EHEKATEMHF FVPGNMVSCL DFVESVFGNA
GNPRLSKNDA ALDPLGWTGH SGMAILAPHL TRMTKKECGL PHISQATERQ KRERMCWEKE
DELYNDGKTF KMYCRDASGV ICTIIADNYF GYCKKEVKTQ ISYSANLYGF AEEEHAGGAV
TRPSYDLGEA CKAVQYAEGY KFSEMVEKNK HSIIVKEEGY AVDKKYPEGI IYVPEDSVFT
IEDASIKFNH NGKEESILLT PKVNYVLPNG YTIILHDTMT SRRWTLRGIL PQYTLCHKPC
TVSGGGKSEI SKNISDAIFE GKMFVNNKEE EFKAVQKVFD HDFSRRYADG EIKSAHILDP
NVTLGTVVKM LTPSSFFTEE HNEFVAAIPP MIVELALTIK SLYREEWKGD WQSRITVDKI
NGKEGHELKY RKMPLPSQYL RVGFERDETT WRVFQLRKDF FPAAKLQMED DITASVIVPT
KLLKTPINTN GKKACKIVKN CELRLFQRPD DAVFRGYDKQ TEYDFSIPGH FISNYQPMTR
EEAKDFTKDV VRLYQYTEPM RKCLQDFVAG KDEAKYIVSS SHTRLVQDGD KLVGSKNPRY
LQRRPDMLDP EYTYMTFKAI QLFRKISDEE PLYTPVDAVL SGRRNNPPQV AKNGMKLRPL
SVFAPLHYFE LPELLMECIT SMTGASPSMF GAGSEGALTK GPFNSLPAVV DLNNYLLGMI
CCGYSGFVSS ASYCGPHYKV AHDISLLIPE IWSRMRRYEQ EPKYLIEHGY LEPCPDVTYN
GKTYSGKRLG YRITKDFTVH YFSSIFSVPN SVMPEDFLKP ELQDLAIYAD SYEYIEQTDK
GIAMNYVKDG TVEGACPPLK ALIYIMANGE YNGMTRESKE FREMFDAKTI LNSEWYKERL
VTRQKLEVAK LNKDLAYLNK TIAEKPRLAE TLNKQIAAVK EELQYVSSEE YLIDIDGSIG
TDPYPYKCMK H
