ID   B2UA06_RALPJ            Unreviewed;      1001 AA.
AC   B2UA06;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 108.
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=Rpic_2572 {ECO:0000313|EMBL:ACD27700.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD27700.1};
RN   [1] {ECO:0000313|EMBL:ACD27700.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=12J {ECO:0000313|EMBL:ACD27700.1};
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., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) 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; CP001068; ACD27700.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2UA06; -.
DR   STRING; 402626.Rpic_2572; -.
DR   KEGG; rpi:Rpic_2572; -.
DR   eggNOG; COG2352; Bacteria.
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:ACD27700.1}.
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        650
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1001 AA;  110583 MW;  35BCCA2994AF6E02 CRC64;
     MTQPAARRAS SRATTARKAS AAPAKTSKAT KAIKAAKPAA KPVAKANGAD 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 AYTSAEELRA DIQIVTDSLA AHHGEALADA RLASLARAID VFGFHLSSID
     LRQVSDVHEA TVAELLKVAG VEGAYAALSE ADKRTLLLRE LQQPRLLTLP FHAYSEQTTQ
     EIDIFRAARE VRARYGNRIV RNYIISHTET LSDLLEVMLL QKEAGMFRAN ANGAGVGLDV
     MVIPLFETIE DLRNASQIMG DLLALPGFDA VLAAQGNEQE VMLGYSDSNK DGGFLTSNWE
     LYKAELALVE LFERKGVRLR LFHGRGGTVG RGGGPTYQAI LSQPPGTVNG QIRLTEQGEI
     ISSKFANPEI GRRNLETIVA ATLEATLLPT RNRPKGLEEF EAAMQALSDN AFAAYRNLVY
     ETPGFKDYFF ATTPITEIAD LNLGSRPASR KLMDKKHRRI EDLRAIPWGF SWGQCRLLLP
     GWFGFGSAVQ RWLDDAGNAK ARAARLTTLK RMHKQWPFFA NLLSNMDMVL SKADLNVASR
     YAQLCDDRKL RNAVFSRISA EFALTEQMLA AITGQSERLA DNPLLARSIK NRFPYLDPLN
     HLQVELLKRF RSGKAGSDDA RVRRGIHLSI NGIAAGLRNS G
//