ID   CAPP_RHOMR              Reviewed;         936 AA.
AC   Q59757;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
GN   Name=ppc; Synonyms=pepC;
OS   Rhodothermus marinus (Rhodothermus obamensis).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Rhodothermus.
OX   NCBI_TaxID=29549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=OKD7 / DSM 12399 / JCM 9785;
RX   PubMed=9276668; DOI=10.1093/oxfordjournals.jbchem.a021737;
RA   Takai K., Sako Y., Uchida A., Ishida Y.;
RT   "Extremely thermostable phosphoenolpyruvate carboxylase from an extreme
RT   thermophile, Rhodothermus obamensis.";
RL   J. Biochem. 122:32-40(1997).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000269|PubMed:9276668}.
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:0000269|PubMed:9276668};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:9276668};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:9276668};
CC       Note=Magnesium. Can also use Mn(2+) instead of Mg(2+).
CC       {ECO:0000269|PubMed:9276668};
CC   -!- ACTIVITY REGULATION: Exhibits positive allosteric property with acetyl-
CC       CoA and fructose 1,6-bisphosphate, and a negative one with L-aspartate
CC       and L-malate. {ECO:0000269|PubMed:9276668}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:9276668};
CC       Temperature dependence:
CC         Optimum temperature is 75 degrees Celsius.
CC         {ECO:0000269|PubMed:9276668};
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; X99379; CAA67760.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59757; -.
DR   SMR; Q59757; -.
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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Carbon dioxide fixation; Lyase; Magnesium; Manganese.
FT   CHAIN           1..936
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166617"
FT   ACT_SITE        155
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        595
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   936 AA;  107886 MW;  C9AA94C3F26C345A CRC64;
     MLPPLQIEIE GTGISRPLSE HVNLLGGLLG QVIQEMAGPE MLELVETLRR LCKQAAQENR
     PEFREQAYTR IHSATYDELL WLLRAYTAFF HLVNQAEQQE IIRINRERAQ QSTPERPRPE
     SIDEAILALK QQGRTLDDVL TLLERLDIQP TVTAHPTEAR RRSILYKQQH IAQMLSQQRR
     CQLTPEEQET LLLDLHNQIT LLLGTAEVRE ERPTVRDEVE QGLYFIQSTI WEAVPRIYED
     VRRALRRYYG ADVDFRPFLR YRSWIGSDRD GNPYVTPEIT RWTALTQRRL ALQRYMEELR
     QLRRRLSLSD RYVAPPEELR RSLARDAREV SLPPHVLRQF RHESFRLKIS YIMGRLHGLL
     QALDDPTQPA PDYDADAFVE DLRLLQRCLE ACGLERIARH DQLTRLLVLA QTFGFHLVTL
     DVRQHSSVHE AAVAELLRLA GVENDYRALP ESRRQELLAE ELSNPRPLLP PGARVSEATR
     QVLETFAVIR ELVQLDPRLV GSYIVSMTHT VSDLLEPMLL AKEVGLWHYE RDPRTGKPGH
     VRCPIDFVPL FETIEDLEAA ASRMEAILSH PVYRMQVAAR GGFQEIMLGY SDSTKDGGYW
     MANWALHRAQ EQLAEVCLRH GVDFRLFHGR GGTVGRGGGR ANQAILAMPP VVHNGRIRFT
     EQGEVISFRY ALPEIAHRHL EQIVNAMLRV VGLPAASGTD GTDPATRNRL MDELAARSMR
     AYRRLIDAPD FWSWYTRITP IDQISRLPIA SRPVSRSSAR EVDFESLRAI PWVFAWTQVR
     YLIPGWFGIG QALDELLQTS PEHLETLRTW YRSWPFFRTV LQNAQREMVR ARLEIAAYYD
     RLLGDGPTAF HQMIEEDYHR ARTAILRITD QESLLDHDPI IRKSVQLRNP YTDVLNLVQL
     ELMRRIRSGA EADREPLRRA LFLSINGIAA AMQSTG