ID   CAPP_RHOPS              Reviewed;         933 AA.
AC   Q139X8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=RPD_1876;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; CP000283; ABE39111.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q139X8; -.
DR   SMR; Q139X8; -.
DR   STRING; 316057.RPD_1876; -.
DR   PRIDE; Q139X8; -.
DR   EnsemblBacteria; ABE39111; ABE39111; RPD_1876.
DR   KEGG; rpd:RPD_1876; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   BioCyc; RPAL316057:RPD_RS09420-MON; -.
DR   Proteomes; UP000001818; 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   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   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium.
FT   CHAIN           1..933
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025586"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        595
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   933 AA;  104371 MW;  F3192417456B66B8 CRC64;
     MSSTILPTDP DVLPNRADDS AFIEEDTRLR NDIRLLGRIL GDTVRDQEGS AVFDLVERIR
     QTSIRFHRDE DKPARRELEA ILDDMSASDT VKIVRAFSYF SHLANIAEDQ NNIRQMRAGS
     TAGSAPRAGM LAKTLAHARE EGIGARELRE FFKTALVSPV LTAHPTEVRR KSTMDREMEV
     AALLDQRERL QLTADEWAQN EEQLRRAVVT LWKTNLLRRT KLTVLDEVAN GLSFYDYTFL
     REVPRLHSAL EDQLGGGEGG EAEEELASFL RMGSWIGGDR DGNPFVTAEV LQGTLRLQSA
     RVLRFYLDEL HELGSELSLA SHLAPITEDV RLLAERSPDH SPHRRHEPYR LAVSGIYARL
     AATAAKLKID SVRAPVGEAE IYANVQEFKA DLDAIHYSLT KYNAGVIARG RLRQLRRAAD
     CFGFHLASLD MRQNSAVHER TMGELMDAAR PTSSYLALDE DERIALLTGE LRSARPLTSI
     FIKYSDETVG ELAVLHEAAR AHSIYGEAAI PQCIISMTKG VSDLLEVAVL LKEVGLIDPS
     GRCAINIVPL FETIEDLQAC AAIMDRLLAI PEYRRLVDSR GGVQEVMLGY SDSNKDGGFV
     TSGWELYKAE IGLLDVFEHH GVRLRLFHGR GGSVGRGGGP SYDAIVAQPG GAVNGQIRIT
     EQGEIITSKY SNREVGRNNL EILTAATLEA SLLQPRRSAP HHDYLEAMEQ LSALAFKAYR
     GLVYETDGFV DYFWSSTVIN EISTLNIGSR PASRKKTRAI EDLRAIPWVF SWAQCRLMLP
     GWYGFGSAVE AWVAEHPDKG TAFLQSMYQE WPFFRMLLSN MDMVLSKSSI AIASRYADLV
     PDEELRHKIF GRIRIEWHAS VDSLLAIMGH ERLLQGNPLL ERSIRHRFPY LDPLNHVQVQ
     LLREHRTHDP DEQVLRGIQL TINGISAGLR NSG