ID G0EUD7_CUPNN Unreviewed; 1012 AA.
AC G0EUD7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
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,
CC ECO:0000256|HAMAP-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; 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 OMA; PWVFGWT; -.
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
//