ID   CAPP_PSEMY              Reviewed;         878 AA.
AC   A4XXP6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
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=Pmen_3360;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
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., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-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; CP000680; ABP86112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4XXP6; -.
DR   SMR; A4XXP6; -.
DR   STRING; 399739.Pmen_3360; -.
DR   KEGG; pmy:Pmen_3360; -.
DR   PATRIC; fig|399739.8.peg.3410; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
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..878
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025578"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        545
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   878 AA;  97128 MW;  CCDCAE0E8362BE08 CRC64;
     MAEIDARLRE EVHLLGELLG QTIRTQLGDD FLDKIERIRK GAKAGRRGSA AGAEQLTSTL
     GDLGDDELLP VARAFNQFLN LANIAEQQHR VRRRRPDEPE PFELRVLDEL LERLLAAGQK
     PDELARQLGR LDIELVLTAH PTEVARRTLI QKYDAIAAQL TALDHSDLLP AERERIAQRL
     QRLIAEAWHT EEIRRSRPSP VDEAKWGFAV IEHSLWQAVP QFLRRADRSL QAATGLRLPL
     EAAPIRFASW MGGDRDGNPN VTARVTREVL LLARWMAADL YLRDVDQLAA ELSMQQASAE
     LRAQVGDSAE PYRALLKQLR ERLRETRSWA QQALTADIAP GAAVLQDNHD LLAPLQLCYQ
     SLHACGMGVI ADGPLLDCLR RAATFGLFLV RLDVRQDSTR HAAALSEITD YLGLGRYAEW
     DEEQRLAFLQ RELDSRRPLL PSDYRPSADT AEVLATCREV AAAPAAALGS YVISMAGAAS
     DVLAVQLLLK EAGLRRPMRV VPLFETLADL DNAGPVIDRL LGLPGYRVRL HGPQEVMIGY
     SDSAKDAGTT AAAWAQYRAQ EELVRLCGEH QVELLLFHGR GGTVGRGGGP AHAAILSQPP
     GSVAGRFRTT EQGEMIRFKF GLPDIAEQNL NLYLAAVLEA TLLPPPAPEP SWRAMMDRLA
     DVGVKAYRGV VREHPQFVAY FRQATPEQEL GRLPLGSRPA KRREGGVESL RAIPWIFAWT
     QTRLMLPAWL GWEQALGQAL AGGEGELLKN MREQWPFFRT RIDMLEMVLA KADASIAALY
     DQRLVEPALQ PLGAQLRDLL SQACAAVLEL TGQSRLLAHS PETLESISVR NTYLDPLHLL
     QAELLARCRL RQQAPESPLE QALLVSVAGI AAGLRNTG
//