ID   CAPP_BORPE              Reviewed;         980 AA.
AC   Q7W0D0;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=BP0215;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(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}.
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DR   EMBL; BX640411; CAE40595.1; -; Genomic_DNA.
DR   RefSeq; NP_879103.1; NC_002929.2.
DR   RefSeq; WP_010929690.1; NZ_CP039021.1.
DR   AlphaFoldDB; Q7W0D0; -.
DR   SMR; Q7W0D0; -.
DR   STRING; 257313.BP0215; -.
DR   KEGG; bpe:BP0215; -.
DR   PATRIC; fig|257313.5.peg.232; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000002676; 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..980
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166582"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        625
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   980 AA;  107774 MW;  E586FA1524F8F745 CRC64;
     MAAYNAPVSN CQFRLTHILP IPQRHGAPTD PFQMNAIRQQ SDSAEPLRHD IRLLGRCLGE
     VIQACEGKRV YDTIETLRRT AVRFRRAGDP ADDKLLQARV KQLRGNDPNS VARAFSYFLH
     LSNIAEDRDQ NRRQRERALA GAGPERGSLR QAIESLKAQG VNNARIRRLL SEACVMPVLT
     AHPTEVQRKS TLDVHREISS LLVQRERELT ADELSELDLA LIGQVATLWQ TRMLRYTRLT
     VADEIENALS YYRSTFLNVI PRVYGDLARL LNREPVKPFT PPPPPLEPFL RMGSWIGGDR
     DGNPNVDAAT LERALLRQAT VLFEHYLQEV HALGAELSAS TLLIEADPAL LALADAGGDD
     SPHRRDEPYR RALIGIYARL AATARHLTGQ KLARRATVPA APYDTPDALA ADLAVIAASL
     SARHGAPIAR LRLSGLQQAV TVFGFHLATV DLRQSSDVHE RVLAELFARA GDGIDGQAVD
     YLALDEAARV AGRELAHARP LASPWIAYSE ETASELAVLR AAAAGRARYG RQAVLQSIVS
     HTETLSDLLE VLVLQKEAGL IAPPGETIAP GDGLMVVPLF ETIPDLQRGP EIMAAWLDLP
     EVRQRVRLAQ GDTQEVMLGY SDSNKDGGFL TSNWSLYQAE RALVDVFSAR SVRLRMFHGR
     GDSVGRGGGS SYDAILAQPP GTVAGQLRLT EQGEVIQSKY KDAEVGRWHL ELLVAATLES
     SLAPQAAATS AEDAHMQQHA PAMSFMSELA QRTYRGLVYD TPGFADYFFA ATPISEIAGL
     NIGSRPASRK KGQHIEDLRA IPWGFSWAQC RLMLTGWYGM GSAIEAYLET GAQGAPRSRR
     ARLAQLREMA SDWPAFRTLL SNMEMVLAKS DLAIAAGYAQ LVPRRGLRER VFGAITAEHG
     RTLAMLRLLT RRDLLADNPG LMASLRERFA YIDPLNYLQI ELIKRHRAAQ RRAGDDADIR
     VPRAIHLTIN GIAAGLRNSG