ID   CAPP_PSEP1              Reviewed;         875 AA.
AC   A5W881;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
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=Pput_4217;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
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., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) 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; CP000712; ABQ80341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5W881; -.
DR   SMR; A5W881; -.
DR   KEGG; ppf:Pput_4217; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
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_1000025579"
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;  96924 MW;  86764AAFF793AD52 CRC64;
     MTDIDVRLRE DVHVLGELLG ETIRQQHGDA FLQKIEDIRH SAKADRRGPG EQLSSTLADL
     AEEDLLPVAR AFNQFLNLAN MAEQYQLIRR RDADQPEPFE AQVLPELLGR LKQAGHSNDA
     LARQLAKLDI QLVLTAHPTE VARRTLIQKY DAIAGQLAAQ DHRDLTSAER QQVRERLRRL
     IAEAWHTEEI RRTRPTPVDE AKWGFAVIEH SLWHAIPSHL RKVDKALLEA TGLRLPLEAA
     PIRFASWMGG DRDGNPNVTA AVTREVLLLA RWMAADLFLR DIDALAAELS MQQANDALRK
     QVGDSAEPYR AVLKQLRDRL RATRAWAHSA LTSNQPAGAD VLVDNRELIA PLELCYQSLH
     ECGMGVIAEG PLLDCLRRAV TFGLFLGRLD VRQDAARHRD ALTEITDYLG LGRYADWDEE
     QRIAFLQAEL KNRRPLLPAH FKPQADTAEV LATCREVAAA PAASLGSYVI SMAGAASDVL
     AVQLLLKEAG LTRPMRVVPL FETLADLDNA GPVMQRLLGL PGYRAGLRGP QEVMIGYSDS
     AKDAGTTAAA WAQYRAQENL VRICAEHQVE LLLFHGRGGT VGRGGGPAHA AILSQPPGSV
     AGRFRTTEQG EMIRFKFGLP GIAEQNLNLY LAAVLEATLL PPPPPQPAWR EVMDQLAADG
     VQAYRSVVRE NPDFVEYFRQ STPEQELGRL PLGSRPAKRR AGGIESLRAI PWIFGWTQTR
     LMLPAWLGWE TALTNALARG QGELLAQMRE QWPFFRTRID MLEMVLAKAD AQIAEAYDER
     LVQPHLRPLG AHLRDLLSQS CQVVLGLTGQ PVLLAHSPET LEFISLRNTY LDPLHRLQAE
     LLARSRSREA ALDSPLEQAL LVTVAGIAAG LRNTG
//