ID   CAPP_BORBR              Reviewed;         982 AA.
AC   Q7WQB3;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 97.
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=BB0420;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
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; 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; BX640438; CAE30918.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7WQB3; -.
DR   SMR; Q7WQB3; -.
DR   KEGG; bbr:BB0420; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000001027; 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   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..982
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166580"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        627
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   982 AA;  108000 MW;  D12349661484A5C3 CRC64;
     MAAYNAPVSN CQFRLTHILP IPQRQGAPTD PFQMNAIRQQ SDSAEPLRHD IRLLGRCLGE
     VIQACEGKRV YDTIETLRRT AVRFRRAGDP ADDKLLQARV KQLRGNDPNS VARAFSYFLH
     LSNIAEDRDQ NRRQRDRALA 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 ELARRATVPA APYDTPDALA ADLAVIAASL
     SAHHGAPIAR LRLSGLQQAV TVFGFHLATV DLRQSSDVHE RVLAELFARA GDGIDGQAVD
     YLALDEAARV AVLRRELAHA RPLASPWIAY SEETASELAV LRAAAAGRAR YGRQAVLQSI
     VSHTETLSDL LEVLVLQKEA GLIAPPGETI APGDGLMVVP LFETIPDLQR GPEIMAAWLD
     LPEVRQRVRL AQGDTQEVML GYSDSNKDGG FLTSNWSLYQ AERALVDVFS ARSVRLRMFH
     GRGGSVGRGG GSSYDAILAQ PPGTVAGQLR LTEQGEVIQS KYKDAEVGRW HLELLVAATL
     ESSLAPQAAA TSAEDAHMQQ HAPAMSFMSE LAQRTYRGLV YDTPGFADYF FAATPISEIA
     GLNIGSRPAS RKKGQHIEDL RAIPWGFSWA QCRLMLTGWY GMGSAIEAYL ETGAQGAPRS
     RRARLAQLRE MASDWPAFRT LLSNMEMVLA KSDLAIAAGY AQLVPRRGLR ERVFGAITAE
     HGRTLAMLRL LTRRELLADN PGLMASLRER FAYIDPLNYL QIELIKRHRA AQRRAGDDAD
     IRVPRAIHLT INGIAAGLRN SG
//