ID   C6BBI5_RALP1            Unreviewed;      1002 AA.
AC   C6BBI5;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=Rpic12D_2167 {ECO:0000313|EMBL:ACS63441.1};
OS   Ralstonia pickettii (strain 12D).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=428406 {ECO:0000313|EMBL:ACS63441.1};
RN   [1] {ECO:0000313|EMBL:ACS63441.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12D {ECO:0000313|EMBL:ACS63441.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Marsh T., Richardson P.;
RT   "Complete sequence chromosome 1 of Ralstonia pickettii 12D.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001644; ACS63441.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6BBI5; -.
DR   STRING; 428406.Rpic12D_2167; -.
DR   KEGG; rpf:Rpic12D_2167; -.
DR   HOGENOM; CLU_006557_2_0_4; -.
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:ACS63441.1}.
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        651
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1002 AA;  110700 MW;  662C03D88DF41549 CRC64;
     MTQPAARRAS SRATTARKAS AAPAKTSKAT KAIKAAKPAA KPVATANGAD EANGASLGPT
     SRRSSGSAAA KDQPLKEDIR FLGRLLGDVL REQEGGAAFE TVETIRQTAV RFRRDGDRQA
     EQELDRLLKA LSREQTNSVV RAFSYFSHLA NIAEDQHHNR RRRVHALAGS PPQPGSMMRA
     LLSVADEGVS GETLRRFFDA ALIVPVLTAH PTEVQRKSIL DAQREIARLL AERDTPLTTR
     ERERNTTLLR AHVTKLWQTR MLRTTRLMVA DEIENALSYY QTTFLREIPA LYRELEEDVA
     AVFPRRGARG EPTPLAPFFQ MGSWIGGDRD GNPFVTAETL RYAARKQASV ILAWYLEEIH
     ALGAELSMST SQVDVSAELL ALAEQSPDRS EHRSDEPYRR ALIGVYARLA ATCRELTGED
     AGRHAVGPAP AYSNAEELRA DIQIVIDSLA AHHGEVLADA RLASLARAID VFGFHLSSID
     LRQVSDVHEA TVAELLKVAG VEGAYAALSE ADKRTLLLRE LQQPRVLTLP FHAYSEQTTS
     EIDIFRAARE VRARYGNRIV RNYIISHTET LSDLLEVMLL QKEAGMFRTG ANGSGSAALD
     VMVIPLFETI EDLRNAPEIM GDLLDLPGFD AVLAAQGNEQ EVMLGYSDSN KDGGFLTSNW
     ELYKAELALV ELFQRKGVRL RLFHGRGGTV GRGGGPTYQA ILSQPPGTVN GQIRLTEQGE
     IISSKFANPE IGRRNLETIV AATLEATLLP TRNRPKGLEE FEAAMQALSD NAFAAYRNLV
     YETPGFKDYF FATTPITEIA DLNLGSRPAS RKLMDKKHRR IEDLRAIPWG FSWGQCRLLL
     PGWFGFGSAV QRWLDDAGNA KARAARLTTL KRMHKQWPFF ANLLSNMDMV LSKADLNVAS
     RYAQLCDDRK LRNAVFSRIS AEFTLTEQML AAITGQSERL ADNPLLARSI KNRFPYLDPL
     NHLQVELLKR FRSGKAGSDD ARVRRGIHLS INGIAAGLRN SG
//