ID   CAPP_PSEPK              Reviewed;         875 AA.
AC   Q88MR4;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 107.
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=PP_1505;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN67126.1; -; Genomic_DNA.
DR   RefSeq; NP_743662.1; NC_002947.4.
DR   RefSeq; WP_010952597.1; NC_002947.4.
DR   AlphaFoldDB; Q88MR4; -.
DR   SMR; Q88MR4; -.
DR   STRING; 160488.PP_1505; -.
DR   PaxDb; 160488-PP_1505; -.
DR   GeneID; 83681961; -.
DR   KEGG; ppu:PP_1505; -.
DR   PATRIC; fig|160488.4.peg.1596; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   PhylomeDB; Q88MR4; -.
DR   BioCyc; PPUT160488:G1G01-1596-MONOMER; -.
DR   Proteomes; UP000000556; 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; Reference proteome.
FT   CHAIN           1..875
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166614"
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;  96964 MW;  173B89B82C761F07 CRC64;
     MTDIDVRLRE DVHVLGELLG ETIRQQHGDA FLQKIEDIRH SAKADRRGPG EQLSSTLADL
     AEEDLLPVAR AFNQFLNLAN MAEQYQLIRR RDADQPEPFE AQVLPELLGR LKQAGHSNDA
     LARQLAKLDI QLVLTAHPTE VARRTLIQKY DAIAGQLAAQ DHRDLTPAER QQVRERLRRL
     IAEAWHTEEI RRTRPTPVDE AKWGFAVIEH SLWHAIPSHL RKVDKALLEA TGLRLPLEAA
     PIRFASWMGG DRDGNPNVTA AVTREVLLLA RWMAADLFLR DIDALAAELS MQQANDTLRK
     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
//