ID   CAPP_BURVG              Reviewed;         997 AA.
AC   A4JGV5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=Bcep1808_2510;
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS   (strain R1808)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=269482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000614; ABO55508.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4JGV5; -.
DR   SMR; A4JGV5; -.
DR   KEGG; bvi:Bcep1808_2510; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000002287; 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..997
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025553"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        649
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   997 AA;  109405 MW;  FADFAC9E2115183C CRC64;
     MKSSGSARTA RRNAALPSTD AQTGALATVA NGRAKPATKP KDSIRQTKRT TKAAGASKPA
     ARTREDKDGP LFEDIRFLGR LLGDVVREQE GDTVFDVVET IRQTAVKFRR EDDSQAAQTL
     EKKLRKLTPE QTVSVVRAFS YFSHLANIAE DRHHNRRRRI HALAGSAPQP GTVAYALEQL
     KTSGNASKRV LQRFFDDALI VPVLTAHPTE VQRKSILDAQ HDIARLLAER DQPLTARERA
     YNESMLRARV TALWQTRMLR DARLTVGDEI ENALSYYRTT FLDELPALYG DIEAALAEHG
     LPARVPAFFQ MGSWIGGDRD GNPNVTAATL DEAINRQAAV ILEHYLEQVH KLGAELSVSN
     LLVGANDAVK ALAAASPDQS PHRVDEPYRR ALIGIYTRLA ASARVRLGEG TVPVRSAGRG
     APPVRAVPYA DSEAFVADLK VLTASLEEHH GASLAAPRLT PLMRAAEVFG FHLSSIDLRQ
     SSDIHEAVVA ELFARAGVHA DYASLSEDDK LIALLAALAD PRPLRSPYIE YSALAQSELG
     VFEKAREVRA QFGPRAVRNY IISHTETVSD LVEVLLLQKE TGLLEGAFGA AHDSARNGLM
     VIPLFETIPD LRDAARIMRE YFALPGIEAL IAHQGAEQEV MLGYSDSNKD GGFLTSNWEL
     YRAELALVDL FRDRKITLRL FHGRGGTVGR GGGPTYQAIL SQPPGTVNGQ IRLTEQGEVI
     ASKFANPEIG RRNLETVVAA TLEASLLPQS NAPAQLPAFE AAMQALSDAA MASYRALVYE
     TPGFTDYFFA ATPITEIAEL NIGSRPASRK LQDPKNRRIE DLRAIPWGFS WGQCRLLLTG
     WYGFGSAVSA YLDGAPDAAA RTKRVALLKK MNKTWPFFAN LLSNMDMVLA KTDLAVASRY
     AQLVADRKLR KHVFERIVAE WERTAQALAE ITGHEGRLAT NPLLARSIKN RFPYLDPLNH
     LQVELIKRHR AGDTNARLRR GIHLTINGIA AGLRNTG
//