ID   CAPP_PSEPG              Reviewed;         875 AA.
AC   B0KS63;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
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=PputGB1_1110;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) 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; CP000926; ABY97018.1; -; Genomic_DNA.
DR   RefSeq; WP_012270799.1; NC_010322.1.
DR   AlphaFoldDB; B0KS63; -.
DR   SMR; B0KS63; -.
DR   KEGG; ppg:PputGB1_1110; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000002157; 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_1000082430"
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;  96876 MW;  F575014741808C5C CRC64;
     MTDIDVRLRE DVHVLGELLG ETIRQQHGDA FLQKIEDIRH SAKADRRGPG EQLSSTLADL
     AEDDLLPVAR AFNQFLNLAN MAEQYQLIRR RDADQPEPFE ARVLPELLAR LKQAGHSNDA
     LARQLAKLDI QLVLTAHPTE VARRTLIQKY DAIAGQLAAQ DHRDLSPAER QQVRERLRRL
     IAEAWHTEEI RRTRPTPVDE AKWGFAVIEH SLWHAIPSHL RKVDKALLEA TGLRLPLEAA
     PIRFASWMGG DRDGNPNVTA AVTREVLLLA RWMAADLFLR DIDALAAELS MQQANDALRE
     RVGDSAEPYR AVLKQLRDRL RATRAWAHSA LASNQPAGAE VLVDNRDLIA PLELCYQSLH
     DCGMGVIAEG PLLDCLRRAV TFGLFLGRLD VRQDAARHRD ALTEITDYLG LGRYADWDEE
     QRIGFLQAEL KNRRPLLPAH FKPQADTAEV LATCREVAAA PAASLGSYVI SMAGAASDVL
     AVQLLLKEAG LTRPMRVVPL FETLADLDNA GPVMQRLLGL PGYRAGLRGP QEVMIGYSDS
     AKDAGTTAAA WAQYRAQENL VRICAEHQVE LLLFHGRGGT VGRGGGPAHA AILSQPPGSV
     AGRFRTTEQG EMIRFKFGLP GIAEQNLNLY LAAVLEATLL PPPPPQPAWR ELMDQLAADG
     VKAYRSVVRE NPDFVEYFRQ STPEQELGRL PLGSRPAKRR AGGIESLRAI PWIFGWTQTR
     LMLPAWLGWE TALSNALARG QGELLAQMRE QWPFFRTRID MLEMVLAKAD AQIAEAYDER
     LVQPHLLPLG AHLRDLLSQS CQVVLGLTGQ PVLLAHSPET LEFISLRNTY LDPLHRLQAE
     LLARSRSREA ALDSPLEQAL LVTVAGIAAG LRNTG
//