ID   D9QL48_BRESC            Unreviewed;       902 AA.
AC   D9QL48;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
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=Bresu_0589 {ECO:0000313|EMBL:ADK99903.1};
OS   Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS   NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=633149 {ECO:0000313|EMBL:ADK99903.1, ECO:0000313|Proteomes:UP000002696};
RN   [1] {ECO:0000313|Proteomes:UP000002696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC   {ECO:0000313|Proteomes:UP000002696};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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; Evidence={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; CP002102; ADK99903.1; -; Genomic_DNA.
DR   RefSeq; WP_013268007.1; NC_014375.1.
DR   AlphaFoldDB; D9QL48; -.
DR   STRING; 633149.Bresu_0589; -.
DR   KEGG; bsb:Bresu_0589; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   InParanoid; D9QL48; -.
DR   OrthoDB; 9768133at2; -.
DR   BioCyc; BSUB633149:G1GM8-588-MONOMER; -.
DR   Proteomes; UP000002696; Chromosome.
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; 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.
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|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:ADK99903.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002696}.
FT   REGION          97..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT   ACT_SITE        571
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   902 AA;  97299 MW;  2FF43F308A238345 CRC64;
     MPVSAEPAAD DRLREEVRLL GGLLGEVIRD EGGQDLYDRI EAVRVASVGY HRHSGARGSA
     ELERLLSDLS LDDAVGLAHG FAVFSLLANV AEDRAGKRRA RSQTAEGARP DTPEGSLARL
     AQAGRSVEDA RTLLSEALIS PVLTAHPSEV RRKSVIDRIA AVSDLLDACD RDDLACAPEV
     MVNGLRRQTV ILWATRLVRT TGLVVQDEID TVVSFLERVF LKVAPEQLID WRRRLNAPDL
     KPFIRIGAWV GGDRDGNPNV DAAALRAAFA TPAKAVLRHY LEAVNTLGAE LSLSGSLAAV
     SPALQALAAS SGDGSPHRAD EPYRRALSQI YARLSATHPL LTGETAPRPA PFAAPPYDGP
     DAFRDDLAVL QDSLVASHGA VFADDGLSRL IATVDVFGFH MATLDLRQNS DVHARVVGHL
     LRVAGVCPDY AALDEEARIA LLSAELAAPR LLFSPYEDYD PEVLKERAIL QAAAEALRTF
     GPQAIRTHIV SKTDAASDLL EVYLLLKEVG LYRHDDPATC PIQAAPLFET IDDLRAAKPT
     LSRLLQEPSA LAVARARGVQ EVMIGYSDSN KDGSYLTSTW ELHEASRALL SVTEAVGVRL
     QLFHGRGGAV GRGGGSSFAG VISQPTGTVA GRIRITEQGE VIANKYGEPD VARRNLDALT
     AGTLIASLAP PPDEAMTAKH GATASALSVA SMAAYRALVY ETPGFVDYFR AATPINEIAE
     LKIGSRPTSR TASSAIEDLR AIPWVLSWSQ SRVMLPGWFG FGSAVRGRDM EELRAMAADW
     PFFRTLLQNM EMIMAKSDMT IARRYAGLVP DQALAASIFG ALRAEWDRTR DAVLAITGQS
     DLLGGQPELD RLIRLRMPYV EPLNHVQIEL IRRRRSGDDD PRVREGILLT INGVAAGLRN
     SG
//