PECK2_ENTHI
ID PECK2_ENTHI Reviewed; 1153 AA.
AC C4M1E4;
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 2 {ECO:0000303|PubMed:26269598};
DE Short=EhPEPCK2 {ECO:0000303|PubMed:26269598};
DE Short=PPi-PEPCK2 {ECO:0000303|PubMed:26269598};
DE EC=4.1.1.38 {ECO:0000269|PubMed:26269598};
DE AltName: Full=Diphosphate-dependent phosphoenolpyruvate carboxykinase 2 {ECO:0000305};
DE AltName: Full=PEP carboxyphosphotransferase 2 {ECO:0000305};
GN Name=PEPCK2 {ECO:0000305};
GN ORFNames=EHI_030750 {ECO:0000312|EMBL:EAL45476.1};
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 PEPCK1 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; DS571208; EAL45476.1; -; Genomic_DNA.
DR RefSeq; XP_650862.1; XM_645770.2.
DR AlphaFoldDB; C4M1E4; -.
DR SMR; C4M1E4; -.
DR STRING; 5759.rna_EHI_030750-1; -.
DR EnsemblProtists; rna_EHI_030750-1; rna_EHI_030750-1; EHI_030750.
DR GeneID; 3405164; -.
DR KEGG; ehi:EHI_030750; -.
DR VEuPathDB; AmoebaDB:EHI5A_126350; -.
DR VEuPathDB; AmoebaDB:EHI5A_194890; -.
DR VEuPathDB; AmoebaDB:EHI5A_252600; -.
DR VEuPathDB; AmoebaDB:EHI_030750; -.
DR VEuPathDB; AmoebaDB:KM1_081510; -.
DR VEuPathDB; AmoebaDB:KM1_309960; -.
DR eggNOG; ENOG502QW6Z; Eukaryota.
DR HOGENOM; CLU_275663_0_0_1; -.
DR InParanoid; C4M1E4; -.
DR OMA; WSKMRRY; -.
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..1153
FT /note="PPi-type phosphoenolpyruvate carboxykinase 2"
FT /id="PRO_0000434731"
FT COILED 1085..1131
FT /evidence="ECO:0000255"
SQ SEQUENCE 1153 AA; 131117 MW; E927C5ECCB86E0D1 CRC64;
MFNQEQGTDY PVLNKKKLES LANLKLAMGG HEYPTDDLTQ QGLKLAGPLL EEVEESEVNH
TTAPIDARLQ TFLNSYFAEC GEEVPKIPDD TFILDREGLG RVLSFPPHKQ EFFCETMKSY
KIKQGVLHNP AKDKRTTVGV FHICQSDVPV PADKIECPKI AFLRMLKAAF YGAPDDHLII
PYTAECKEPT RSWVSLYMRP VVVPGVKGVK GFEHEKATEM HFFVPGNMVS CLDFVESVFG
NAGNPRLSKN DAALDPLGWT GHSGMAILAP HLTRMTKKEC GLPHISQATE RQKRERMCWE
KEDELYNDGK TFKMYCRDAS GVICTIIADN YFGYCKKEVK TQISYSANLY GFAEEEHAGG
AVTRPSYDLG EACKAVQYAE GYKFSEMVEK NKHSIIVKEE GYAVDKKYPE GIIYVPEDSV
FTIEDASIKF NHNGKEESIL LTPKVNYVLP NGYTIILHDT MTSRRWTLRG ILPQYTLCHK
PCTVSGGGKS EISKSIRDAV IEGSVFVNNK EEDFKAVQEI FDHDFSKRYA NGEVKPIHIL
DPNVTLGTVV ELLTPSHLFT KEHNDYISSI SPLIVELVMT IKSLYREDWK GDWQSRITVD
KINGNEGNEL KYRGANLCSQ YLRVGFERDE TTWRVFQLRK DFFPAAKLQM EDDITASVIV
PTKLLKTPIN NMQKKACKIV KNCELRLFQR PDDAVFRGFD KQTEYDFSIP GHFISNYQPM
TREEAKDFTK DVVRLYQYTE PMRKCLQDFV AGKDEAKYIV SSSYTRLVPE GDKLVGSKNP
RYLQRRPDML DPEYTYMTFK AIQLYRKISD EEPLYTPVDA VLSGRRNNPP QVAKNGMKLR
PLSVFAPLHY FELPELLMEC ITSMTGASPS MFGAGSEGAL TKGPFNSLPA VVDLNNYLLG
MICCGYSGFV SSASYCGPHY KVAHDISLLI PEIWSKMRRY EQEPKYLIEH GYLEPCPDVT
YNGKTYSGKR LGYRITTAFA NHFLRTLFSM PNSVMPEDFL KPELQDLAIY ADSYEYMSQT
DKGIAMNYVK DGTVEGACPP LKALIYIMAN GEYNGMTRES KEFREMFDPE VVLNSEWYKE
RLVTRQKLEV AKLNKDLAYL NKTIAEKPRL VETLNKQIAA VKEELQYVSS EEYLIDIDGS
IGTDPYPYKC MKH
