ID   CAPP_RHOPB              Reviewed;         929 AA.
AC   Q218E3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
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};
GN   OrderedLocusNames=RPC_1684;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18;
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., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000301; ABD87243.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q218E3; -.
DR   SMR; Q218E3; -.
DR   STRING; 316056.RPC_1684; -.
DR   KEGG; rpc:RPC_1684; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
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; Lyase; Magnesium.
FT   CHAIN           1..929
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025585"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        591
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   929 AA;  103875 MW;  F75692E00EA9B814 CRC64;
     MSSKIMPIDP IAQKTPVAED PAAIDEDARL RDDIRLLGRI LGDTVRDQEG EGVFDVVERI
     RQTSIRFHRD NDKPARSELE AILDGLSTPD TVRIVRAFSY FSHLANIAED QNNIRQMRAL
     SGTPRPGSVV GTLAHARAVG ISAQELRRFF AHALVSPVLT AHPTEVRRKS TMDREMEVAG
     LLDRRERLQM TAEEVAQHEE QLRRAVLTLW QTNMLRRTKL TVLDEVKNGL SFYDHSFLRE
     VPRLHGLLED RLNDDDGRDE ELASFLRMGS WIGGDRDGNP FVTAEVMRGA LRLQSTRALR
     FYLDELHALG SELSIAAHLA DVSDDLRLLA ERSPDTSPHR SGEPYRLAVS GIYARLAATA
     HKLKFDDIRA PVGAAEPYAD PQEFKADLDV LHRSLIANQA SVIARGRLRQ LRRAVDCFGF
     HLASLDMRQN SAVHERTMTE LIDAAMPGKS YMAMNEEARI ALLAGELRST RPLASPFVKY
     GEETLGELAV FRTAAEAHAA FGHTVISQCI ISMCKGVSDM LEVVLLLKEV GLVDHAGRSA
     INVVPLFETI EDLQASAGIM DRLLSLHDYR RLVDSRGGVQ EVMLGYSDSN KDGGFVTSGW
     ELYKAEIELV KVFEHHGVRL RLFHGRGGSV GRGGGPSYDA ILAQPGGAVN GQIRITEQGE
     IITSKYSNAE VGRNNLEILA AATLEASLLM PRQSAPRAEY LDAMEQLSSF AFKAYRGLVY
     ETEGFEDYFW ASTVITEIAT LNIGSRPASR KKTHKIEDLR AIPWVFSWAQ CRLMLPGWYG
     FGSAVEAFVK EHPDKGMAFL QELYREWPFF RTLLSNMDMV LAKSSIAIAS RYAELVPDEQ
     LRQAIFGRIR AEWHGSIQAL LDIMQQDRLL QSNPRLERSI RNRFPYLDPL NHVQVELLKE
     HRSHAIDEKV LRGIQLTING ISAGLRNSG
//