ID   F4QE77_CACFS            Unreviewed;       923 AA.
AC   F4QE77;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   ORFNames=DFA_11786 {ECO:0000313|EMBL:EGG14024.1};
OS   Cavenderia fasciculata (Slime mold) (Dictyostelium fasciculatum).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Acytosteliales;
OC   Cavenderiaceae; Cavenderia.
OX   NCBI_TaxID=261658 {ECO:0000313|EMBL:EGG14024.1, ECO:0000313|Proteomes:UP000007797};
RN   [1] {ECO:0000313|Proteomes:UP000007797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH3 {ECO:0000313|Proteomes:UP000007797};
RX   PubMed=21757610; DOI=10.1101/gr.121137.111;
RA   Heidel A.J., Lawal H.M., Felder M., Schilde C., Helps N.R., Tunggal B.,
RA   Rivero F., John U., Schleicher M., Eichinger L., Platzer M., Noegel A.A.,
RA   Schaap P., Gloeckner G.;
RT   "Phylogeny-wide analysis of social amoeba genomes highlights ancient
RT   origins for complex intercellular communication.";
RL   Genome Res. 21:1882-1891(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; GL883029; EGG14024.1; -; Genomic_DNA.
DR   RefSeq; XP_004350732.1; XM_004350681.1.
DR   AlphaFoldDB; F4QE77; -.
DR   STRING; 1054147.F4QE77; -.
DR   EnsemblProtists; EGG14024; EGG14024; DFA_11786.
DR   GeneID; 14865688; -.
DR   KEGG; dfa:DFA_11786; -.
DR   OMA; FGWTQSR; -.
DR   Proteomes; UP000007797; Unassembled WGS sequence.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
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:UP000007797}.
FT   ACT_SITE        152
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        588
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   923 AA;  104595 MW;  42B4AF3DD262A738 CRC64;
     MLGPLDFGIV EKDELDRDID KLRNILQDSI KELEKSGDGE QLIKDVKELL LAETPSERTP
     EFMEKFIEKV SSLSNESALR ISRTLSHCLN LANVAEQTHL IRSVKNLESE EEGVLKFSCE
     DIFKQLIEAG VEPDRIYKAL TEQSIELVLT AHPTQMMRRT LITKNNHIGE ALEGLSNKSQ
     SSRDRKDWED QLRREISGSW LTDEIRRNKP TPLEEAQGGF SILEQNLWRT LPKFMKVLDR
     TCFKYTGKNL PLGFTNIKFG SWMGGDRDGN DNVNSKVTKQ VSYFSRWIAA SLFYKEIDAL
     LFELSMVRMT PELAEAALKA QERRNTNRPK PVLTLYKEFG GGSGIPEREG YRILLAEMRD
     KMLLTKKHYE DLIGGQTPPP DHDDDDIYHT AKQVLDPLLL CYDSLISVGA IDVANGRLID
     VIRQLNCFGL TLSKLDIRQE STRHSEVLDA ITNYLGIGSY LSWNEKERQE FLIRELESKR
     PLVPKDLPCN ARVQEVLDTF RMAAELPAES LGAYVISMCQ NPSDILAVEL LQKESGNKFP
     QRVAPLFEMI DDLERAPQTM EQLYSIKWYK DRINGSQEIM LGYSDSSKDS GRLTSSWSLY
     KAQEILTKLS DKHGVKLTLF HGRGGTIGRG GAPTYLAIQS QPGGSINGRL RVTEQGEMIT
     AHYGQPGVAF RSIEVYTTAT LQQTLLPPPP PSDHWREIMD ELSSVSGKKY RSIVRGNENF
     VRYFRASTPE RELSHLNIGS RPQKRNVSGG IESLRAIPWI FAFTQTRLIL PAWLGVAEAL
     EAAKEKGYTN DLKEMYKSWP YFQTTIDLIE MVLMKADPLI AARYNDLLVP FELQSLGKEM
     IGLLNKTVSS ILSLTNHSTL QQDNKLLQHF IAIRRSYLDP LNYIQAEVLR RLRSNHVEAQ
     NPILVDILII SINGLAAGLR NTG
//