ID   CAPP_RHOP5              Reviewed;         927 AA.
AC   Q07QP5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=RPE_1791;
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53;
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., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-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; CP000463; ABJ05739.1; -; Genomic_DNA.
DR   RefSeq; WP_011663224.1; NC_008435.1.
DR   AlphaFoldDB; Q07QP5; -.
DR   SMR; Q07QP5; -.
DR   STRING; 316055.RPE_1791; -.
DR   EnsemblBacteria; ABJ05739; ABJ05739; RPE_1791.
DR   KEGG; rpe:RPE_1791; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
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..927
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025584"
FT   ACT_SITE        160
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        589
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   927 AA;  103076 MW;  A4BAE8574C8419D7 CRC64;
     MSSTVLSVEP DALPRSGEDA AAIAEDARLR DDIRLLGRIL GDTVRDQEGE DVFDAVERIR
     QTSIRFHRDN DQPARDELVE LFDGLSTPAT LRIVRAFSYF SHLANLAEDQ NNIRQMRLQN
     GARPGSLVAT LAHARAVGIS AKELRHFFET ALVSPVLTAH PTEVRRKSTM DREMEIARLL
     DRRERLQMTP EEIEQHEELL RRAVLTLWQT NMLRRTKLTV LDEVANGLSF YDYAFLHEVP
     RLHGVLEDKL NDDDGAGEEL ASFLRMGSWI GGDRDGNPFV TAEVMRGTLR LQSRRALRHY
     LDELHALGSE LSIAAHLADI SDELRALAEN SPDTSPHRAG EPYRLAVSAI YARLAATAHR
     LGIDDIRAPV AESAPYAEPA ELKADLDVLH RSLVANNSAV IARGRLRSLR RAVDCFGFHL
     ASLDMRQNSA VHERTMAELI DKAMPGKSYM AMNEEARIAL LAAELRSPRP LASPFVKYSE
     ETVDELAVFR AAAEAHATFG PAAIPQCIIS MTKGVSDLLE VVVLLKEVGL VDPAGRSAIN
     VVPLFETIED LQAAAGIMDR LLGLHDYRRL VDSRGGVQEV MLGYSDSNKD GGFVTSGWEL
     YKAEIELLKI FEHHGVRMRL FHGRGGSVGR GGGPSYDAIL AQPAGAVNGQ IRITEQGEII
     TSKYSNPEVG RNNLEVLAAA TLEASLLQPR LGAPCVGYLK AMDEISALAF KAYRGLVYET
     EGFEDYFWSS TVITEIATLN IGSRPASRKK THKIEDLRAI PWVFSWAQCR LMLPGWYGFG
     SAVEAWVKAH PEQGMAYLQE LNREWPFFRT LLSNMDMVLS KSSIAIASRY AELVADEKLR
     AAIFGRIKRE WHSSIAALLA IMGHQRLLQG NPRLERSIRH RFPYLDPLNH VQVELLKQHR
     DHAVDEQALR GIQITINGIS AGLRNSG