ID   E1TBJ5_BURSG            Unreviewed;      1090 AA.
AC   E1TBJ5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=BC1003_0917 {ECO:0000313|EMBL:ADN56901.1};
OS   Burkholderia sp. (strain CCGE1003).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN56901.1};
RN   [1] {ECO:0000313|EMBL:ADN56901.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN56901.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome1 of Burkholderia sp. CCGE1003.";
RL   Submitted (SEP-2010) 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; CP002217; ADN56901.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1TBJ5; -.
DR   STRING; 640512.BC1003_0917; -.
DR   KEGG; bgf:BC1003_0917; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
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:ADN56901.1}.
FT   REGION          1..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        300
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        742
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1090 AA;  118792 MW;  DF520293283C3455 CRC64;
     MTSSGSARSA RRNTASPNAS TADAGAFPAS ATIAADAASA GKVKRATSGA KAATASQAAK
     AEKASNAATT TKALKAGKAG KTSLPVKADK AGKADKAGKA VKADNEDKAL KMPKPGKSSE
     AVPSTKKKGE AAGPTPALPA VSADAPPPAP KTNGRTRDDK DHPLFQDIRY LGRLLGDVLR
     EQEGDEVFDV VETIRQTAVR FRREDDNAAA QTLDKKLRSL SPEQTVSVVR AFSYFSHLAN
     IAEDRHRNRR HRIHALAGSA AQPGSIAYAL ERLVEAGAAA TPVLQQFFND ALIVPVLTAH
     PTEVQRKSIL DAEHDVARLL AERDQQLTER ERAHNETMLR ARVTSLWQTR MLRDSRLTVA
     DEIENALSYY RATFLEEIPA LYADIEEALK EHGLEARLPP FFQMGSWIGG DRDGNPNVTA
     ETLEHAIARQ AEVIFEHYLE QVHKLGAELS VSNLLAGASD ELKALADISP DRSPHRTDEP
     YRRALIGMYT RLAASARVRL GEGSVPLRSA GRGAAPIRAT PYDDASEFVR DLHVLIDSLA
     AHHGAPLAAP RLAPLARAAE VFGFHLASID LRQSSDIHEA VIAELLKRAG VHDDYAALSE
     SEKLAVLLAE LAQPRPLRLP YAEYSDLVKS ELGVLEQARV TREKFGARAV RNYIISHTET
     VSDLVEVMLL QKETGLLQGQ LGNPNDPAKA ALMVIPLFET IPDLRNAPHI MRDLLALPGA
     DSIIEHQGNE QEVMLGYSDS NKDGGFLTSN WELYRAELAL VSLFNERGIT LRLFHGRGGT
     VGRGGGPTYQ AILSQPPGTV DGQIRLTEQG EVIASKFGNP EIGRRNLETV VAATLEASLL
     PHGNAPAELP AFEETMQQLS DAAMASYRAL VYETPGFKEY FFESTPISEI AELNIGSRPA
     SRKLQDPKHR KIEDLRAIPW GFSWGQCRLL LTGWYGFGSA VGAYLDGAPS DTERARRLAL
     LKKMHKSWPF FSTLLSNMDM VLAKTDLAVA SRYAALVSDK KLRKHVFERI VAEWERTSKV
     LSEISGKSER LAENPLLARS IKNRFPYLDP LNHLQVELLK RHRAGDTNAR VRRGIHLTIN
     GIAAGLRNTG
//