ID   CAPP_XANCP              Reviewed;         904 AA.
AC   Q8P336;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=XCC0754;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(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; AE008922; AAM40069.1; -; Genomic_DNA.
DR   RefSeq; NP_636145.1; NC_003902.1.
DR   RefSeq; WP_011035990.1; NC_003902.1.
DR   AlphaFoldDB; Q8P336; -.
DR   SMR; Q8P336; -.
DR   STRING; 190485.XCC0754; -.
DR   EnsemblBacteria; AAM40069; AAM40069; XCC0754.
DR   KEGG; xcc:XCC0754; -.
DR   PATRIC; fig|190485.4.peg.822; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
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..904
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166652"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        570
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   904 AA;  100146 MW;  FD2409710F896A1F CRC64;
     MNEYRSSLVF ATPDVPLRDD VRRLGALVGD LLAEQVSADF LEEIERIRTT AIARRESDTP
     PAGLLSLLEG REPRAAEALV RAFSTYFQVV NIAERVHRIR RRRDYQRSGT DTPQPEGLHD
     ALRRLKAQGV TLDELSEWLP RIDVEPVFTA HPTEAVRRAL LEKEQLMVAS LVDNLDGMRT
     PNERATDAAR FRMALTASWQ TADSSPVRPT VEDEREHVGF YLTQVLYRVI PVMYETLEHA
     IEETYGSTLA LPRLLRFGTW VGGDMDGNPN VDAHTIAGTL DAQRRAVLDR YLNELWQLAS
     LLSQSTTLVA VSPALSAQLE RYQALLPDAA ARSRPRHGDM PYRLLNDLMR ARLQATLDDA
     DGAYAAPAEL EHDLQLILDS LEVNKGLHAG WFAVRRLLWR VRSFGFHLAR LDVRQESSVH
     ARAVADALGQ ADWDSQDATH RAGLLGPYAS GEQALPQVDD EGNARLDAVF AALADARTRH
     GADALGSYII SMAHNRADVL TVLALARRGG LVDDAGAVPL DIVPLFETVD DLRGGTGTVQ
     DLLADPVYRQ HLRARGDTQM VMLGYSDSGK DGGIAASRWG LQRAQVELLE AAAELGVRLT
     FFHGRGGSIV RGGGKTTRAL DAAPRGSVDG RLRVTEQGEV IHRKYGIRAL ALRSLEQMTG
     AVLLSSLRPR APEPREDAWR PVMDLVAERS TVAYRGFVGA PDFMQYFRLA TPIDVIERMT
     LGSRPSRRLG QDAALSNLRA IPWVFAWSQA RAVIPGWYGV GSGLQAAVEA GHEDSLREMA
     QDWPFFRTFL DDIAMVLSKG DLNIAELFSR LAGPLHARFF PRIRDELALT KHWVKTLLGQ
     RSLLQHDPRL ALSIRLRNPY IDPISVLQVD LLQRWRATDG EDEELLRALV ACVNGVAQGV
     QNTG
//