ID   CAPP_PSEPF              Reviewed;         876 AA.
AC   Q3KHE4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=Pfl01_1069;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA72812.1; -; Genomic_DNA.
DR   RefSeq; WP_011332655.1; NC_007492.2.
DR   AlphaFoldDB; Q3KHE4; -.
DR   SMR; Q3KHE4; -.
DR   KEGG; pfo:Pfl01_1069; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000002704; 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..876
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025580"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        543
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   876 AA;  97375 MW;  F0D64E1CEF9206F2 CRC64;
     MTDIDARLRE DVHLLGELLG NTIRDQYGEA FLDKIEQIRK GAKADRRGSM DAELSASLNQ
     LSEDELLPVA RAFNQFLNLA NIAEQYQLIH RREETQAAPF ESRVLPELLA RLRNEGHSAE
     SLARQLARLE IELVLTAHPT EVARRTLIQK YDAIAAQLAA QDHRDLTTAE REQIHNTLQR
     LIAEAWHTEE IRRTRPTPVD EAKWGFAVIE HSLWQAIPHH MRKADQALFA ATGLRLPLEA
     APIRFASWMG GDRDGNPNVT AAVTREVLLL ARWMAADLYL RDVDHLAAEL SMQQASDALK
     ARAGDSAEPY RAVLKQLRER LRATRNWAHA SLTATTPAPA DVLHNNRDLL DPLELCFNSL
     HECGMGVIAD GPLLDCLRRA VTFGLFLVRL DVRQDSSRHS AAMTEITDYL GLGKYEEWDE
     EQRISFLTRE LQNRRPLLPA HFKPSADTAE VLATCKEIAA APGASLGSYV ISMAGAASDV
     LAVQLLLKES GVLRPMRVVP LFETLADLDN AGPVIERLLL LPGYRARLQG PQEVMIGYSD
     SAKDAGTTAA AWAQYRAQER LVEICREQQV ELLLFHGRGG TVGRGGGPAH AAILSQPPGS
     VAGRFRTTEQ GEMIRFKFGL PDIAEQNLNL YLAAVLEATL LPPPPPTPEW RHLMDELAAD
     GVAAYRAVVR ENPQFVEYFR QSTPEQELGR LPLGSRPAKR RAGGIESLRA IPWIFGWTQT
     RLMLPAWLGW ETALSKALER GEGELLGQMR EQWPFFRTRI DMLEMVLAKA DADIALSYDE
     RLVEPDLLPL GAHLRDLLSQ ACSVVLGLTG QSQLLAHSPD TLEFIRLRNT YLDPLHLLQA
     ELLARSRRQN VEQGSPVEQA LLVSVAGIAA GLRNTG
//