ID   CAPP_BURPS              Reviewed;         994 AA.
AC   Q63W75;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=BPSL1013;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH35009.1; -; Genomic_DNA.
DR   RefSeq; WP_004191560.1; NZ_CP009538.1.
DR   RefSeq; YP_107641.1; NC_006350.1.
DR   AlphaFoldDB; Q63W75; -.
DR   SMR; Q63W75; -.
DR   STRING; 272560.BPSL1013; -.
DR   GeneID; 56596175; -.
DR   KEGG; bps:BPSL1013; -.
DR   PATRIC; fig|272560.51.peg.555; -.
DR   eggNOG; COG2352; Bacteria.
DR   Proteomes; UP000000605; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..994
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166585"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        646
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   994 AA;  108735 MW;  55D70FE099C4A788 CRC64;
     MKSSGSARAT RRNAVSSSSA PAHAEPPARR AAKPARKLDG AAARPLAPTN AASAKPQGRT
     REDKDRPLFE DIRYLGRLLG DVVREQEGDA VFDVVETIRQ TAVKFRREDD KAAAQTLEKM
     LRKLTPEQTV SVVRAFSYFS HLANIAEDRH HNRRRRIHAL AGSAAQAGTV AYALDKLKQA
     GDASSKTIKQ FFEGALIVPV LTAHPTEVQR KSILDAQHDI ARLLAERDQP LTARELAHNE
     ALLRARVTTL WQTRMLRDAR LTVADEIENA LSYYRATFLD ELPALYADIE EALAEHGLRA
     RVPAFFQMGS WIGGDRDGNP NVTAATLDEA ISRQAAVIFE HYLEQVHKLG AELSVSNLLV
     GASDALKALA AASPDQSPHR VDEPYRRALI GVYTRLAASA RVRLGEGTVP VRSAGRGAAP
     VRATPYADAE EFAADLRVLT DSLALHHGES LATPRLAPLM RAAEVFGFHL ASIDLRQSSD
     IHEAVVAELL ARGGVEADYA ALPEADKLRV LLAALADPRP LRSPYLDYSD LAKSELGVLE
     RAHAIRAQFG ARAVRNYIIS HTETVSDLVE VLLLQKETGL FEGTLGTPHA NARNGLMVIP
     LFETIADLRN ASDIMRAFFA LPGVGELLAH QGHEQEVMLG YSDSNKDGGF LTSNWELYRA
     ELALVDLFDE RGIKLRLFHG RGGTVGRGGG PTYQAILSQP PGTVNGQIRL TEQGEVIASK
     FANPEIGRRN LETVVAATLE ATLAPHSNAP KQLPAFEAAM QTLSDAAMAS YRALVYETPG
     FTDYFFSSTP ITEIAELNIG SRPASRKLQD PKNRKIEDLR AIPWGFSWGQ CRLLLTGWYG
     FGSAVAAYLD GAPDAAERGK RVALLKKMNK TWPFFANLLS NMDMVLAKTD LAVASRYAQL
     VADKKLRKHV FERIVAEWHR TADALAEITG AHARLAANPL LARSIKNRFP YLDPLNHLQV
     ELIKRHRAGD TNARLRRGIH LTINGIAAGL RNTG
//