ID   CAPP_XANOM              Reviewed;         904 AA.
AC   Q2NZE4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=XOO3578;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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}.
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DR   EMBL; AP008229; BAE70333.1; -; Genomic_DNA.
DR   RefSeq; WP_011260202.1; NC_007705.1.
DR   AlphaFoldDB; Q2NZE4; -.
DR   SMR; Q2NZE4; -.
DR   KEGG; xom:XOO3578; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
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..904
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025603"
FT   REGION          52..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  100268 MW;  05288ABD914227E2 CRC64;
     MNEYRSSLVF ATPDLPLRDD VRRLGALVGD LLAEQVSAEF LDEIERVRTT AISRRESDAP
     PSTLSEQLTG REPRDAEALV RAFSTYFQVV NIAERVHRIR RRREYQRSGT DTPQPDGLHD
     ALRRLKAQGV TLDELSQWLP RIDVEPVFTA HPTEAVRRAL LEKEQLMVAS LVDNLDGMRT
     PNERTSDAAR FRMALTASWQ TADSSPVRPT VGDEREHVGF YLTQVLYRVI PVMYETLEHA
     IEETYGSVPA LPRLLRFGTW VGGDMDGNPN VDANTIAGTL DAQRRAVLDR YQKELWQLAS
     LLSQSTTLVQ VSPELMTQLE RYRALLPDAA ARSRPRHGDM PYRLLNDLMR ARLQATLDDA
     DGAYTAPSEL EDDLQLILDS LQANKGLHAG WFAVRRLLWR VRSFGFHLAR LDVRQESSVH
     ARAVADALGQ TDWDAQDATR RAAVLGPYAC GQEALPRVQD EGNARLDAVF AALADARTRH
     GADALGSYII SMAHNRADVL TVLALARRGG LVDAAGAVPL DIVPLFETVD DLRGGTGTVQ
     DLLADPVYRQ HLAARGDTQM VMLGYSDSGK DGGIAASRWG LQRAQVELLE AAADLGVRLT
     FFHGRGGSIA RGGGKTSRAL DAAPRGSVDG RLRVTEQGEV IHRKYGIRAL ALRSLEQMTG
     AVLLSSLRPR APEPREARWR PVMDLVAERS TVAYRAFVAA PEFMQYFRLA TPIDVIERMT
     LGSRPSRRLG QDAALSNLRA IPWVFAWSQA RAVIPGWYGV GSGLQAAVDA GHEDSLREMA
     QDWPFFRTFL DDVAMVLSKG DLNIAELFSR LSGDLHTRFF PLIRDELALT KGWVKALLQQ
     QSLLQHDPRL ALSIRLRNPY IDPISVLQVD LLQRWRATDG EDEALLRALV ACVNGVSQGL
     QNTG
//