ID   F0ZJ70_DICPU            Unreviewed;       919 AA.
AC   F0ZJ70;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   ORFNames=DICPUDRAFT_97713 {ECO:0000313|EMBL:EGC36009.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC36009.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001071};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346}.
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DR   EMBL; GL871040; EGC36009.1; -; Genomic_DNA.
DR   RefSeq; XP_003287447.1; XM_003287399.1.
DR   AlphaFoldDB; F0ZJ70; -.
DR   STRING; 5786.F0ZJ70; -.
DR   EnsemblProtists; EGC36009; EGC36009; DICPUDRAFT_97713.
DR   GeneID; 10500353; -.
DR   KEGG; dpp:DICPUDRAFT_97713; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   InParanoid; F0ZJ70; -.
DR   OMA; FGWTQSR; -.
DR   OrthoDB; 355614at2759; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001064}.
FT   ACT_SITE        152
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        584
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   919 AA;  104944 MW;  07896515B6D0845F CRC64;
     MPNENPYDFG VLSVPDDLDR DIEKLRNILW ESIKELEEDG EEIIKKASEL ILETPPSERT
     KEFIDQYTHK ISSLSNVDSL KISRIFSQFL NLINVAEQHH LIRSVRNTFL NGEQLNYSCE
     EVFEQLLSKG LTPDQVYDAI LKQNIELVLT AHPTQIMRRT MISKNNAIGE ALALIDNKTL
     TGFEREDANK SLLREIGGSW LTDEIRRSKV TVEMEAHGGF SVIEQTLWQA IPKFIKILDR
     CCEKYLKKNL PPAFVNVKIA SWMGGDRDGN PNVNAETTKS ISYFSRWIAS TLYYKEIDAL
     LFELSMIKKN KKLEEYSKQS MERRQGNKLR YLTTLYKEFK EGIPSRECYR IVLAEIRDKM
     LLTKRKYEDL IAGLPVNYAP GDTYEYASEV LEPLQICYDS LVEVGAESVA NGRLLDNIRR
     LSCFGLTLSK MDIRQESSRH TDVIDCITQY LGLGSYREWD EKKKQDFLIL ELENKRPLIP
     DDLPCSPEVK EVLSTFKMAA NLSDESLGAY VISMCQSPSD ILAVHLLQKE AGNKHPQRVV
     PLFETATDLD NAPKTMEALF KLPWYIKAIS GEQEIMLGYS DSAKDAGRLT SAWELYKAQE
     ILANLCDKFN VKLTLFHGRG GSIGRGGGSA HEGIMSQPGG SLRGTIRITE QGETINSHYG
     QLGVALRTIE LYTTAVLKQT LTPPPPPTDK WREIMEHLSM ASCKKYRSIT KENPNFIKYF
     RTSTVQPEMI HLNIGSRPSK RAAQFSVDSI RAIPYIFSFT QNRLILPVWL GIEEAIKEAK
     SKNWEDNLRT MYNEWPFFRT LIDLVEMVLM KTDPQIAQRY NELLVPFENQ SLGEELVKEL
     QITIDAVLGL TKHKTLQEDN QILQHFVSIR RSYMDVCNYI QAETLRRLRS SHVDSQDPLL
     VDTLIITFNG ISSGMKNTG
//