ID   Q47F75_DECAR            Unreviewed;       918 AA.
AC   Q47F75;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=Daro_1759 {ECO:0000313|EMBL:AAZ46506.1};
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ46506.1};
RN   [1] {ECO:0000313|EMBL:AAZ46506.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RCB {ECO:0000313|EMBL:AAZ46506.1};
RA   Salinero K.K., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S.,
RA   Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT   "Complete sequence of Dechloromonas aromatica RCB.";
RL   Submitted (AUG-2005) 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; CP000089; AAZ46506.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47F75; -.
DR   STRING; 159087.Daro_1759; -.
DR   KEGG; dar:Daro_1759; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
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:AAZ46506.1}.
FT   ACT_SITE        147
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        580
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   918 AA;  101964 MW;  EC3340717DF1C2CE CRC64;
     MHDASPSKDE PLRTDIRLLG RILGDTVREQ EGESVFDIVE RVRQTAVRFA RDGDPAARDE
     LAALLDPLPG DTTQAVVRAF SYFLQLANIA EDEHHIRRRR AHDLAGSPPR EGSLIFALDA
     LSTAAVSPEA IADFFAHAVV APVLTAHPTE VQRQSLIRNH RDLAHLLDQR ERLQMTPEEE
     AENDLALANA ILTLWQSRML RPVRLKVLDE VKNGITYFKE TFFTELPRLY IQATEQLQKR
     YPEKTWALPP FFRVGSWIGG DRDGNPFVTA DILREALRLQ SSAALNHYLN EVHELGGELP
     LSDLLVKVTP ELLALAEHST DHSPQRADEP YRRALSGIYA RLAATARALD QFEPVRHEIG
     HATPYDTPDA LRADLKLLAN SLKLNGSAKL AGGRLRRLLR GVQIFGFHLA PIDLRQNSDV
     HARSVAELLA GAGRCPDYEA LSEAERIKLL VDEISTPRPL YSPYLNYSEE TQGELAIFFA
     ARELRQKYGS AALPNCIISK TDGVSDLLEL ALLLKESGLL LPGAKPQLKV NIIPLFETIE
     DLQKSAATMA GVFAIPAYRE LIAGRGDEHE VMLGYSDSNK DGGFLTSGWE LYKAEIELAR
     IFGQHGVRLR LFHGRGGSVG RGGGPTYHAI LAQPAGAVAG QIRLTEQGEV ISTKYGNADT
     GRRNLEVLLA ATLEASLTDH ENRVEPAEQF HAVMDELSAR AFNAYRGLVY ETPGFTTYFR
     QSTVVSEIAS LNIGSRPASR KASERIEDLR AIPWVFSWAQ CRLMLPGWYG FGAAVEGYLQ
     ANPAGLATLR RMVHAWPFFK SLLSNMDMVL AKTDLAIASR YAELVADVEL REHIFSRIKA
     EWALTRQHLL AILEQDEFLA DNPLLARSLQ LRSPYMDPLN HLQVELLKRH RAGDTDERLA
     RGIHLTINGI ASGLRNSG
//