ID   CAPP_RHOP2              Reviewed;         933 AA.
AC   Q2IU23;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-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=RPB_3592;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-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; CP000250; ABD08287.1; -; Genomic_DNA.
DR   RefSeq; WP_011442471.1; NC_007778.1.
DR   AlphaFoldDB; Q2IU23; -.
DR   SMR; Q2IU23; -.
DR   STRING; 316058.RPB_3592; -.
DR   KEGG; rpb:RPB_3592; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008809; 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   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..933
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025583"
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;  103411 MW;  7CBDE6697042F794 CRC64;
     MSSMILPTEP EALPNRADDS AALEAETRLR NDIRLLGRIL GDTVRDQEGA AVFDLVEGIR
     QTSIRFHRDD DTTARRELEA ILDGMSASDT VKIVRAFSYF SHLANIAEDQ NNIRQMRVGS
     TAGSAPRAGM LAKTLAHARA DGIGAAELRD FFKTALVSPV LTAHPTEVRR KSTMDREMQI
     AALLDERERV QLTPEEWEQN EEQLRRAVVT LWKTNLLRRT KLTVLDEVTN GLSFYDYTFL
     REVPRLHCAL EDQLGGGEGA EADAELASFL RMGSWIGGDR DGNPFVTAEV LHGTLQLQSA
     RVLRFYLDEL HELGSELSLA SHLVAISDEV RALAERSPDH SPHRRHEPYR LAVSGIYARL
     AATAAKLRID SIRAPVGEAE AYASVHDFKA DLDAIHRSLV AHNAGVIARG RLRQLRRAAD
     CFGFHLASLD MRQNSAVHER TIAELMNAAH PASAYLEIGE DARIALLTAE LRSARPLTSI
     FVKYSDETVG ELAVLHEAAQ AHATYGAAAI PQCIISMTKG VSDLLEVAVL LKEVGLIDPS
     GRSAINIVPL FETIEDLQAS SAIMDRLLGI PEYRRLVDSR GGVQEVMLGY SDSNKDGGFV
     TSGWELYKAE IGLIEIFEHH GIRLRLFHGR GGSVGRGGGP SYDAIVAQPG GAVNGQIRIT
     EQGEIITSKY SNREVGRNNL EILTAATLEA SLLQPKRVAP QRDYLDAMEQ LSAMAFKAYR
     GLVYETDGFV DYFWASTVIT EISTLNIGSR PASRKKTRAI EDLRAIPWVF SWAQCRLMLP
     GWYGFGSAVE AWIAAHPDKG VPFLRSMYQE WPFFRTLLSN MDMVLSKSSL GIASRYAELV
     PDETLRREIF GRIRAEWHAS VDGLLAIMGH DKLLQGNPLL DRSIRHRFPY LDPLNHVQVQ
     LLREHRTHDP DEQILRGIQL TINGISAGLR NSG
//