ID   CAPP_PSEE4              Reviewed;         875 AA.
AC   Q1IDV2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-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=PSEEN1264;
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK14157.1; -; Genomic_DNA.
DR   RefSeq; WP_011532573.1; NC_008027.1.
DR   AlphaFoldDB; Q1IDV2; -.
DR   SMR; Q1IDV2; -.
DR   STRING; 384676.PSEEN1264; -.
DR   GeneID; 32804541; -.
DR   KEGG; pen:PSEEN1264; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000658; 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..875
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025576"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        542
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   875 AA;  97058 MW;  A7AF30F8F3A4FAD9 CRC64;
     MSDIDQRLRE DVHLLGELLG ETIRQQHGEA FLQKIEDIRH SAKADRRGEG EQLSSTLGDL
     AEEDLLPVAR AFNQFLNLAN IAEQYQLIHR RDTDQPEPFE ARVLPELLAR LKAAGHGNDA
     LARQLARLDI QLVLTAHPTE VARRTLIQKY DAIAAQLAAQ DHRDLIPAER QQVRERLRRL
     IAEAWHTEEI RRTRPTPVDE AKWGFAVIEH SLWQAVPNHL RKVDKALFEA TGLRLPLESA
     PVRFASWMGG DRDGNPNVTA AVTREVLLLA RWMAADLFLR DIDYLAAELS MQQASGALRE
     QVGDSAEPYR ALLKQLRDRL RATRAWAHAS LAGPQPASAA VLVDNRDLIA PLELCYQSLH
     ACGMGVIADG PLLDSLRRAV TFGLFLVRLD VRQDAARHRD ALSEITDYLG LGRYADWDEE
     RRIEFLQHEL KNRRPLLPAH FKPAAETAEV LATCREIAAA PAASLGSYVI SMAGAASDVL
     AVQLLLKEAG LTRPMRVVPL FETLADLDNA GPVMERLLGL PGYRAGLHGP QEVMIGYSDS
     AKDAGTTAAA WAQYRAQENL VRICREHQVE LLLFHGRGGT VGRGGGPAHA AILSQPPGSV
     GGRFRTTEQG EMIRFKFGLP GIAEQNLNLY LAAVLEATLL PPPPPEPAWR ALMDQLAADG
     VKAYRGVVRD NPEFVEYFRQ STPEQELGRL PLGSRPAKRR AGGIESLRAI PWIFGWTQTR
     LMLPAWLGWE TALSNALARG QADLLAQMRE QWPFFRTRID MLEMVLAKAD AQIAEAYDQR
     LVQPRLLPLG AHLRDLLSQS CQVVLGLTGQ QVLLAHSPET LEFIRLRNTY LDPLHRLQAE
     LLARSRSREA ALDSPLEQAL LVTVAGIAAG LRNTG
//