ID   Q1LJQ3_CUPMC            Unreviewed;      1009 AA.
AC   Q1LJQ3;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 109.
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:ABF09623.1};
GN   OrderedLocusNames=Rmet_2750 {ECO:0000313|EMBL:ABF09623.1};
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF09623.1, ECO:0000313|Proteomes:UP000002429};
RN   [1] {ECO:0000313|Proteomes:UP000002429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC   {ECO:0000313|Proteomes:UP000002429};
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000352; ABF09623.1; -; Genomic_DNA.
DR   RefSeq; WP_011517323.1; NC_007973.1.
DR   AlphaFoldDB; Q1LJQ3; -.
DR   STRING; 266264.Rmet_2750; -.
DR   KEGG; rme:Rmet_2750; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000002429; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        216
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        659
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1009 AA;  111760 MW;  77C57A2AABF86506 CRC64;
     MTQPAARPTG RSRSTGRKSV TPASGQLDPE GASPKTPKAT KPRTKAAARP KLAVVAAKGA
     APTAAATTIP ARRTADKDLP LREDIRFLGR LLGDCVREQE GDAAFDLVET IRQTAVRFRR
     ENDRAAGTEL DRLLKRLSRD QTNSVVRAFS YFSHLANIAE DQHHNRRRRV HALAGSPPQP
     GSLSRALQAI DAAGVTGKQL REFLDDALIM PVLTAHPTEV QRKSILDAER EIARLLAERD
     LPMTTRERDH NTAQLRARVT TLWQTRMLRN TRLMVVDEIE NALSYYRTTF LQGIPRLMAE
     LEEDIAEVFP RRSKTGATPA PLAPFLQMGS WIGGDRDGNP NVTAETLEHA ARQQATLLFD
     WYLDELHALG AELPLSSLMV DASPELLALA EASPDHSEHR ADEPYRRALI GMYARLAATS
     QLLTGHVAQR HPVADVAPYE NAEAFAADVQ IVVDSLRTHH GEALARGRVD ALVRAIAVFG
     FHLASIDMRQ VSDVHEAVIA ELFATAGIES DYAALPEARK LELLLAELRQ PRLLTLPWHD
     YSEQTRSELA IFAMARDLRA RYGARIARNY IISHTETLSD LIEVMLLQKE AGMLRGTLGS
     KTDPARMELM VIPLFETIED LRNAAGIMES LLDLPGFDSV IAHHGVEQEV MLGYSDSNKD
     GGFLTSNWEL YKAELALVKL FEERRVKLRL FHGRGGTVGR GGGPTYQAIL SQPPGTVNGQ
     IRLTEQGEII NSKFANAEIG RRNLETVIAA TLEASLLPTQ NAPKDLATFE GVMQQLSDHA
     FSAYRDLVYE TPGFKDYFFA TTPITEIADL NLGSRPASRK LMDKKHRRIE DLRAIPWGFS
     WGQCRLLLPG WFGFGSAVQA LLDAAPDEKS RKATVATLKR MVKSWPFFST LLSNMDMVLA
     KTDLAVASRY AGLCEDTALR KAVFSRISAE WHLTSDMLGL ITGRQERLAD NPLLARSIKN
     RFAYLDPLNH LQVELLKRYR AGKDGDDVRV RRGIHLTING VAAGLRNSG
//