ID   CAPP_PSESM              Reviewed;         878 AA.
AC   Q886R9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=PSPTO_1508;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016853; AAO55028.1; -; Genomic_DNA.
DR   RefSeq; NP_791333.1; NC_004578.1.
DR   RefSeq; WP_011103582.1; NC_004578.1.
DR   AlphaFoldDB; Q886R9; -.
DR   SMR; Q886R9; -.
DR   STRING; 223283.PSPTO_1508; -.
DR   EnsemblBacteria; AAO55028; AAO55028; PSPTO_1508.
DR   GeneID; 1183145; -.
DR   KEGG; pst:PSPTO_1508; -.
DR   PATRIC; fig|223283.9.peg.1529; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   PhylomeDB; Q886R9; -.
DR   Proteomes; UP000002515; 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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 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..878
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166615"
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;  97649 MW;  F5CAC7F8929C84F3 CRC64;
     MADIDARLRE DVHLLGELLG NTIREQRGAE FLDKIERIRK GAKAGRRGSA EGAEQLSSSV
     DGLEDDELLP VARAFNQFLN LANIAEQYQL MHRRDDAQPL PFESRVLSEL LDRLKAEGHQ
     PETLARQLSK LEIELVLTAH PTEVARRTLI QKYDAIATQL AALDHRDLNS AERAQITSRL
     QRLIAEAWHT EEIRRIRPTP VDEAKWGFAV IEHSLWHAIP NYLRKADHVL HAATGLHLPL
     ESAPIRFASW MGGDRDGNPN VTAAVTREVL LLARWMAADL YLRDVDNLAA ELSMQQASDA
     LRASVGDSAE PYRAELKRLR ERLRATRNWA NASLTETLPA PEAVLRDNRE LLDPLLLCFQ
     SLHECGMGVI ADGPLLDCLR RAVTFGLFLV RLDVRQDSTR HCAAMTEITD YLGLGRYEEW
     DEQTRIDFLL RELNNRRPLL PSYFKPAADT AEVLATCREV AAAPAASLGS YVISMAGSAS
     DVLAVQLLLK ESGLQRPMRV VPLFETLADL DNAGPVIETL LGLPGYRSRL QGPQEVMIGY
     SDSAKDAGTT AAAWAQYRAQ EKLVEICREQ QVELLLFHGR GGTVGRGGGP AHAAILSQPP
     GSVAGRFRTT EQGEMIRFKF GLPDIAEQNL NLYLAAVLEA TLLPPPPPQP AWRTMMDQMA
     SDGVSAYRAV VRENPEFVEY FRQATPEQEL GRLPLGSRPA KRREGGVESL RAIPWIFAWT
     QTRLMLPAWL GWEAALSKAL ERGEGEVLAQ MREQWPFFRT RIDMLEMVLA KADADIARLY
     DERLVTAELQ HLGAHLRDLL SQACNVVLGL TGQTQLLAHS PETLEFISLR NAYLDPLHLL
     QAELLSRSRN REASLDSPLE LALLVSVAGI AAGLRNTG