ID   E3JCU0_PSEI1            Unreviewed;       968 AA.
AC   E3JCU0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=FraEuI1c_1878 {ECO:0000313|EMBL:ADP79930.1};
OS   Pseudofrankia inefficax (strain DSM 45817 / CECT 9037 / DDB 130130 / EuI1c)
OS   (Frankia inefficax).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Pseudofrankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP79930.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP79930.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Beauchemin N., Sen A.,
RA   Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|HAMAP-Rule:MF_00595}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP002299; ADP79930.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3JCU0; -.
DR   STRING; 298654.FraEuI1c_1878; -.
DR   KEGG; fri:FraEuI1c_1878; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   InParanoid; E3JCU0; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002484; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
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, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:ADP79930.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        624
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   968 AA;  104207 MW;  0A1AD86F05FEECB3 CRC64;
     MTAMDHRGEA RTSGAGSDPG PGTEQGLNSE HGPNSEQSLD AGTFAGGVAS DVRHAGVRAG
     VRRLGQLLGE SLTRHEGAQL LELVERVRAL ARDSGDRADL HRVLADVDHP TAIVLARAFT
     AYFQLANITE QLHRARELAD RPRGAIEETG GRIAAAVAAG QLDPELPAQV VSRLELRPVF
     TAHPTEASRR SVLDVLRGIA ELLDAADDPR AQPSRRAVVD RRLAEAVDVL WQTDELRVER
     PKPTDEARSA AYYLTSIATD VLPGLLEELD GALAQVGAGL PITARPLRFG TWAGGDRDGN
     PNVTPTVTLD VLTLQHEFGI RVLLGAVDGL IKDLTASTRV VEVSDELVAS LDADRAAHPE
     VYDRFIRLNA AEPYRLKASY LRARLAATRD RLAAGTAHVP GRDYLSLRGL LADLTVMHRS
     LMDNRGQLVA DGPLRRTIRV AAAVGMSLAT LDIREHGERH HAALGALYDR LDELPRPYAD
     LDRHERIALL SRELAGRRPL SGAAAPAPAD PTAAAVLELF ATIRVALDRF GEDVIESYIV
     SMTRDVDDIL AVVVLAREAG LLEITPGAGA RARIGFVPLF ETVAELRAAG RLLDGMLADP
     SYRAVVAARG DLQEIMLGYS DSSKDAGITA SQWEIHRAQR ELRDVARRHG VVLRLFHGRG
     GSVGRGGGPT GEAILAQPFG TLDGPIKVTE QGEVISDKYT LPQLARHNLE IALAAVLEAS
     ILHRESRQPL DVLAEWDQTM EAVADSARTA YRALTTDPAL VPFFLAATPV DELGHLNIGS
     RPSRRPGGVG GLEDLRAIPW VFGWTQSRII LPGWFGLGTG LAAARAAGAG DTLAEMYRSW
     HFFRTFLSNV SMTLAKTDLR IASDYVTTLV PAEKAGPFEV IRAEHERTVA EVLAVTGSAT
     LLEHAPVLRQ TLEVRDLYLA PLHALQVSLL ARSRAAAQTD PGGEIDPRLR RALLLTINGI
     AAGLRNTG
//