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,
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}.
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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
//
