ID   CAPP_XANAC              Reviewed;         904 AA.
AC   Q8PP82;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   25-MAY-2022, 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=XAC0806;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
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;
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAM35694.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008923; AAM35694.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015462881.1; NC_003919.1.
DR   AlphaFoldDB; Q8PP82; -.
DR   SMR; Q8PP82; -.
DR   STRING; 190486.XAC0806; -.
DR   EnsemblBacteria; AAM35694; AAM35694; XAC0806.
DR   GeneID; 66909998; -.
DR   KEGG; xac:XAC0806; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000000576; 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.
FT   CHAIN           1..904
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166651"
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;  100154 MW;  B531033622FEEEA5 CRC64;
     MNEYRSSLVF ATPDLPLRDD VRRLGALVGD LLAEQVSAEF LDEIERVRTT AISRRESDAP
     PSTLSEQLAG RQPRDAEALV RAFSTYFQVV NIAERVHRIR RRREYQRSGT DTPQPDGLHD
     ALRRLKAQGV TLDELSQWLP RIDVEPVFTA HPTEAVRRAL LEKEQLMVAS LVDNLDGMRT
     PNERASDAAR FRMALTASWQ TADSSPVRPT VDDEREHVGF YLTQVLYRVI PVMYETLEHA
     IEETYGSVPA LPRLLRFGTW VGGDMDGNPN VDAKTIAGTL DAQRRAVLDR YQKELWQLAS
     LLSQSTTLVQ VSGELTAQLE RYRALLPDAA ARSRPRHGDM PYRLLNDLMR ARLQATLDDA
     DGAYAAPSEL EHDLQLILDS LQANKGLHAG WFAARRLLWR VRSFGFHLAR LDVRQESSVH
     ARAVADALGQ TDWDAQDATQ RAAVLGPYAA GQDPLPRVDD EGNARLDAVF AALADARTRH
     GADALGSYII SMAHNRADVL TVLALARRGG LVDDAGAVPL DIVPLFETVD DLRGGTGTVQ
     DLLADPVYRQ HLAARGDTQM VMLGYSDSGK DGGIAASRWG LQRAQVELLE AAAELGVRLT
     FFHGRGGSIA RGGGKTSRAL DAAPRGSVDG RLRVTEQGEV IHRKYGIRAL ALRSLEQMTG
     AVLLSSLRPR APEPREARWR PVMDLVAERS TVAYRAFVGA PEFMQYFRLA TPIDVIERMT
     LGSRPSRRLG QDAALSNLRA IPWVFAWSQA RAVIPGWYGV GSGLQAAVDA GHEETLREMA
     QDWPFFRTFL DDIAMVLSKG DLNIAELFSR LSGDLHTRFF PLIRDELALT KGWVKALLQQ
     QSLLQHDPRL ALSIRLRNPY IDPISVLQVD LLQRWRATDG EDEALLRALV ACVNGVSQGV
     QNTG