ID   G0EUD7_CUPNN            Unreviewed;      1012 AA.
AC   G0EUD7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
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:AEI78184.1};
GN   OrderedLocusNames=CNE_1c28710 {ECO:0000313|EMBL:AEI78184.1};
OS   Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS   / N-1) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI78184.1, ECO:0000313|Proteomes:UP000006798};
RN   [1] {ECO:0000313|EMBL:AEI78184.1, ECO:0000313|Proteomes:UP000006798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC   {ECO:0000313|Proteomes:UP000006798};
RX   PubMed=21742890; DOI=10.1128/JB.05660-11;
RA   Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT   "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL   J. Bacteriol. 193:5017-5017(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;
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; CP002877; AEI78184.1; -; Genomic_DNA.
DR   RefSeq; WP_013957758.1; NC_015726.1.
DR   AlphaFoldDB; G0EUD7; -.
DR   KEGG; cnc:CNE_1c28710; -.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   Proteomes; UP000006798; 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};
KW   Pyruvate {ECO:0000313|EMBL:AEI78184.1}.
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        215
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        662
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1012 AA;  112111 MW;  FD36B6708A2E6DAA CRC64;
     MTQHAARPHG RRTAPAAKDQ SPALGAGQGD ANGASTTESK RPATRSGTKR SPKPKLSIVS
     SNGTAIAPTA RRTADKDVPL REDIRFLGRL LGECLREQEG DAAFEVVETI RQTAVRFRRE
     NDRAAGAELD RLLKRLSRDQ TNQVVRAFSY FSHLANIAED QHHNRRRRVH ALAGSPPQAG
     SLAHALEAID AAGVTGKQLR KFLDEALIVP VLTAHPTEVQ RKSILDAERE IARLLAERDL
     PMTAREREHN TAQLRAKVTT LWQTRMLRDS RLTVADEIEN ALSYYRTCFL RGIPQLMSEL
     EEDIAAVFPA TRKRKGTPGA QPAPLAPFLQ MGSWIGGDRD GNPNVTAETL EHAASQQGQM
     IIDWYLDEVH ALGAELSMST LMVDASPELL ALAERSPDHS EHRADEPYRR ALIGIYARLA
     ATSKALTGHA VPRRPVAPAE PYDSAEAFAA DVQVVVDSLR ANHGQALANG RIDALARAIG
     VFGFHLASVD MRQVSDVHEA VIAELFAAAG IAPDYAALPE ARKLELLLAE LRQPRLLTLP
     WHEYSEQTRK ELAIFAAARE LRARYGKRIA RNYIISHTET LSDLVEVMLL QKESGMLQGT
     LGSKTDPARM ELMVIPLFET IEDLRNAAGI MQSLLDLPGF DSVIAHHGVE QEVMLGYSDS
     NKDGGFLTST WELYKAELAL VQLFEQRQVK LRLFHGRGGT VGRGGGPTYQ AILSQPPGTV
     NGQIRLTEQG EIINSKFANA EIGRRNLETV VAATLEASLL PQQNAPRELD TFEAVMQQLS
     DRAFTAYRDL VYETPGFKDY FFATTPITEI ADLNLGSRPA SRKLMDKKNR RIEDLRAIPW
     GFSWGQCRLL LPGWYGFGSA VKSLLDTAPD DKARKLAVTT LRRMVKTWPF FSTLLSNMDM
     VLAKTDLAVA SRYAQLCDDA ALRRTVFNRI SKEWHLTCEM LTLVTGHQER LADNPLLARS
     IKNRFAYLDP LNHLQVELLK RFRSGKDGDD IRVRRGIHLT INGVAAGLRN TG
//