ID   Q2T072_BURTA            Unreviewed;      1088 AA.
AC   Q2T072;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
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   ECO:0000313|EMBL:ABC37498.1};
GN   OrderedLocusNames=BTH_I0871 {ECO:0000313|EMBL:ABC37498.1};
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC37498.1, ECO:0000313|Proteomes:UP000001930};
RN   [1] {ECO:0000313|EMBL:ABC37498.1, ECO:0000313|Proteomes:UP000001930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC   {ECO:0000313|Proteomes:UP000001930};
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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; CP000086; ABC37498.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2T072; -.
DR   KEGG; bte:BTH_I0871; -.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000001930; Chromosome I.
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..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        740
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1088 AA;  118811 MW;  E1F173592EEA1F07 CRC64;
     MVARASRATA RLAGCASGPH GLRQDPERSF GSRRHPASAS GSGPPPPHRS PRRPVSSTDA
     PARAVQRAPP HRLIALAVAG PQFPFTRAFP RKSIVKSSGS ARATRRNAVS SSSAPANAEL
     PARRAAKTAR KPNGAAARTI APTNAASAKP HGRTREDKDR PLFEDIRYLG RLLGDVVREQ
     EGDAVFDVVE TIRQTAVKFR REDDKTAAQT LEKMLRKLTP EQTVSVVRAF SYFSHLANIA
     EDRHHNRRRR IHALAGSAPQ AGTVAYALDK LRQAGDASSK TIKQFFEGAL IVPVLTAHPT
     EVQRKSILDA QHDIARLLAE RDQPLTARER AHNEALLRAR VTTLWQTRML RDARLTVADE
     IENALSYYRA TFLDELPALY TDIEEALAEH GLPARVPAFF QMGSWIGGDR DGNPNVTAAT
     LDEAINRQAA VIFEHYLEQV HKLGAELSVS NLLVGASDAL KALAAASPDQ SPHRVDEPYR
     RALIGVYTRL AASARVRLGE GAVPVRSAGR GAAPVRATPY ADAEEFVADL RVLTDSLAVH
     HGESLATPRL APLMRAAEVY GFHLASIDLR QSSDIHEAVI AELLARGGVE PDYAALPEAD
     KLRVLLAALA DPRPLRSPYL DYSDLAKSEL GVLERAHAIR AQFGARAVRN YIISHTETVS
     DLVEVLLLQK ETGLFEGTLG APHANARNGL MVIPLFETIA DLRNASDIMR EFFALPGVGE
     LLAHQGHEQE VMLGYSDSNK DGGFLTSNWE LYRAELALVD LFHERGIKLR LFHGRGGTVG
     RGGGPTYQAI LSQPPGTVNG QIRLTEQGEV IASKFANPEI GRRNLETVVA ATLEATLAPH
     SNAPKQLPAF EAAMQTLSDA AMASYRALVY ETPGFTDYFF SSTPITEIAE LNIGSRPASR
     KLQDPKHRKI EDLRAIPWGF SWGQCRLLLT GWYGFGGAVA AYLDGAPDAA ERGKRVALLR
     KMNKTWPFFA NLLSNMDMVL AKTDLAVASR YAQLVADKKL RKHVFERIVA EWHRTASALA
     EITGAQARLA ANPLLARSIK NRFPYLDPLN HLQVELIKRH RAGDTNARLR RGIHLTINGI
     AAGLRNTG
//