ID   B1JWR1_BURO0            Unreviewed;      1009 AA.
AC   B1JWR1;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Bcenmc03_2430 {ECO:0000313|EMBL:ACA91591.1};
OS   Burkholderia orbicola (strain MC0-3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex;
OC   Burkholderia orbicola.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA91591.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|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:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP000958; ACA91591.1; -; Genomic_DNA.
DR   RefSeq; WP_012329001.1; NC_010508.1.
DR   AlphaFoldDB; B1JWR1; -.
DR   GeneID; 83049220; -.
DR   KEGG; bcm:Bcenmc03_2430; -.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000002169; 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 {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:ACA91591.1}.
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        219
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        661
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1009 AA;  110805 MW;  2AB5F1909ADD0788 CRC64;
     MKSSGSARTA RRNAALPSPD ASTDTVATAA NGRAKTAAKP TATKPKDPIR QTKRTTKAAS
     PAARNAVAPK AGTRTRDNKD GPLFEDIRFL GRLLGDVVRE QEGDTVFDVV ETIRQTAVKF
     RREGDSEAAQ TLEKKLRKLT PEQTVSVVRA FSYFSHLANI AEDRHHNRRR RIHALAGSAP
     QPGTVAYALD QLKTTGNASK RLLQRFFDDA LIVPVLTAHP TEVQRKSILD AQHDIARLLA
     ERDQELTARE RQYNETMLRA RVTALWQTRM LRDARLTVGD EIENALSYYR ATFLDELPAL
     YGDIEAALAE HGLSARVPAF FQMGSWIGGD RDGNPNVTAA TLDEAINRQA AVILEHYLEQ
     VHKLGAELSV SNLLVGANDA VKALAAASPD QSPHRVDEPY RRALIGIYTR LAASARVRLG
     EGTVPVRSAG RGAPPVRAIP YEDSEAFVAD LKVLTASLDE HHGASLAAPR LAPLVRAAEV
     FGFHLASIDL RQSSDIHEAV VAELFARAGV EADYAALAEE DKLRVLLAAL ADPRPLRSPY
     LEYSALAQSE LGVFEKAREV RAQFGARAVR NYIISHTETV SDLVEVLLLQ KETGLLEGTL
     GVPGSHAKNS LMVIPLFETI PDLRDASRIM RDYFALPGID ALIAHQGAEQ EVMLGYSDSN
     KDGGFLTSNW ELYRAELALV DLFRERKITL RLFHGRGGTV GRGGGPTYQA ILSQPPGTVN
     GQIRLTEQGE VIASKFSNPS IGRRNLETVV AATLEASLLP QSNAPAQLPA FEAAMQTLSD
     SAMAAYRALV YETPGFTDYF FSSTPITEIA ELNIGSRPAS RKLQDPKQRK IEDLRAIPWG
     FSWGQCRLLL TGWYGFGSAV SAYLDGAQDD AERAKRVTLL KKMNKTWPFF ANLLSNMDMV
     LAKTDLAVAS RYAQLVSDRK LRKHVFERIV AEWERTSRAL AEITGQEGRL ATNPLLARSI
     KNRFPYLDPL NHLQVELIKR HRAGDTNARL RRGIHLTING IAAGLRNTG
//