ID   Q39DW9_BURL3            Unreviewed;      1008 AA.
AC   Q39DW9;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=Bcep18194_A5753 {ECO:0000313|EMBL:ABB09347.1};
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957 {ECO:0000313|EMBL:ABB09347.1, ECO:0000313|Proteomes:UP000002705};
RN   [1] {ECO:0000313|Proteomes:UP000002705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383
RC   {ECO:0000313|Proteomes:UP000002705};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) 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; CP000151; ABB09347.1; -; Genomic_DNA.
DR   RefSeq; WP_011352872.1; NC_007510.1.
DR   AlphaFoldDB; Q39DW9; -.
DR   GeneID; 45095637; -.
DR   KEGG; bur:Bcep18194_A5753; -.
DR   PATRIC; fig|482957.22.peg.2732; -.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000002705; 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}.
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        218
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        660
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1008 AA;  110609 MW;  E1B17BA931229DF8 CRC64;
     MKSSGSARTA RRNAALSSSD ASTDTVATAA NGRAKTATKP KDPIRQTKRT AKAAGPAART
     AARTAAAPKS GTRTREDKDG PLFDDIRFLG RLLGDVVREQ EGDTVFDVVE TIRQTAVKFR
     REDDSEAAQT LEKKLRKLTP EQTVSVVRAF SYFSHLANIA EDRHHNRRRR IHALAGSASQ
     PGTVAYALEQ LKTTGNASKR LLQRFFDDAL IVPVLTAHPT EVQRKSILDA QHDIARLLAE
     RDQELTGRER QYNESMLRAR VTALWQTRML RDARLTVGDE IENALSYYRA TFLDELPALY
     GDIEAALAEH GLSARVPAFF QMGSWIGGDR DGNPNVTAPT LEEAINRQAA VILEHYLEQV
     HKLGAELSVS NLLVGANDAV KALAAASPDQ SPHRVDEPYR RALIGIYTRL AASARVRLGE
     GTVPVRSAGR GAAPVRATPY ADSEAFVADL KVLTASLDEH HGTSLAAPRL APLVRAAEVF
     GFHLASIDLR QSSDIHEAVV AELFARAGVE ADYAALAEED KLRVLLAALA DPRPLRSPYF
     EYSALAQSEL GVFEKAREVR AQFGARAVRN YIISHTETVS DLVEVLLLQK ETGLLDGALG
     VPGGDAKNSL MVIPLFETIP DLRDAARIMR EYFALPGIDA LIAHQGAEQE VMLGYSDSNK
     DGGFLTSNWE LYRAELALVD LFRDRKITLR LFHGRGGTVG RGGGPTYQAI LSQPPGTVNG
     QIRLTEQGEV IASKFANPEI GRRNLETVVA ATLEATLLPQ NNAPAQLPAF EAAMQTLSDS
     AMAAYRALVY ETPGFTDYFF SSTPITEIAE LNIGSRPASR KLQDPKQRKI EDLRAIPWGF
     SWGQCRLLLT GWYGFGSAVS AYLDGAQDDA ERTKRVALLK KMNKTWPFFA NLLSNMDMVL
     AKTDLAVASR YAQLVSDRKL RKHVFERIVA EWERTSQALA EITGHEGRLA TNPLLARSIK
     NRFPYLDPLN HLQVELIKRH RAGDTNARLR RGIHLTINGI AAGLRNTG
//