ID   F5Y5T8_RAMTT            Unreviewed;       951 AA.
AC   F5Y5T8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-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:AEG93972.1};
GN   OrderedLocusNames=Rta_28690 {ECO:0000313|EMBL:AEG93972.1};
OS   Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 /
OS   TTB310).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG93972.1, ECO:0000313|Proteomes:UP000008385};
RN   [1] {ECO:0000313|Proteomes:UP000008385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC   {ECO:0000313|Proteomes:UP000008385};
RA   Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., Py B.,
RA   Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., Marechal E.,
RA   Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., DuBow M.,
RA   Barras F., Heulin T.;
RT   "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEG93972.1, ECO:0000313|Proteomes:UP000008385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC   {ECO:0000313|Proteomes:UP000008385};
RX   PubMed=21912644; DOI=10.1371/journal.pone.0023784;
RA   De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C.,
RA   Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O.,
RA   Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V.,
RA   Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I.,
RA   Vermeglio A., Achouak W., Heulin T.;
RT   "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome
RT   Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment.";
RL   PLoS ONE 6:E23784-E23784(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}.
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; CP000245; AEG93972.1; -; Genomic_DNA.
DR   RefSeq; WP_013902203.1; NC_015677.1.
DR   AlphaFoldDB; F5Y5T8; -.
DR   STRING; 365046.Rta_28690; -.
DR   KEGG; rta:Rta_28690; -.
DR   PATRIC; fig|365046.3.peg.2939; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008385; 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   Pyruvate {ECO:0000313|EMBL:AEG93972.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008385}.
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        606
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   951 AA;  106067 MW;  1291D6E1616C106D CRC64;
     MSAPANRPAA PPPEAPAATP GRRARDNEKP LAEDIRLLGR ILGDVIREQE GVAAFELVER
     IRKLSVAFRR DADQDADRAL KTLLKSLSGD QAVSVIRAFT YFSHLANLAE DRHHIRRRVI
     HERAGDTHEG SIEVALARLR WAGISPRAIA TSLAHSYVSP VLTAHPTEVQ RKSILDAERG
     IARLLAERDE VKARALPKDA LAPRELAANE AQIRARVLQL WQTRLLRFTK LTVADEIENA
     LSYYEATFLR EIPKLYAGLE RELGRESVAS FLRMGMWIGG DRDGNPHVGA DTLDYALRRQ
     SEVALRHYLT EVHWLGAELS HSAMLVDVTP AMRRLADSSP DVNEHRMDEP YRRALAAMYA
     RLAATLKLFT GGEAARHALA PQNPYPAAAD FLADLCTIRD SLLADHGEAI VAQRLHPLIR
     AVEVFGFHLA TMDLRQSSDQ HEAVVAELLA TARIEAHYGK LQEQARRDLL VKLLCDARPL
     RVVGAAYSDH AQRELAIFET ARRLRAQYGR EAIRHYIISH TESVSDLLEV LLLQKEVGLM
     RGTLDDAGVA DLIVVPLFET IEDLRNAAPI MREFYALPGV VALVQRSHSG GYGEQDIMLG
     YSDSNKDGGI FTSNWELYRA EIALVELFDS LPPAHRIRLR MFHGRGGTVG RGGGPSYQAI
     LAQPPGTVRG QIRLTEQGEV IGSKYANPEI GRRNLETLVA ATLEATLLQP TKPAPPAFLE
     AAEALSRASM KAYRALVYEA PGFTEYFQGA TPIREIAELN IGSRPASRKS SQRIEDLRAI
     PWSFSWGQCR LTLPGWYGFG SAVHAFLHEN AAQPRKEALA LLQKMYRQWP FFRALLSNID
     MVLAKSDLAL ASRYAELVAD TRLRKRIFAA IEAEWQRTVE ALQLITGERQ RLAGNPALQR
     SIRHRFPYID PLHHLQVELV RRWREGKADE RVQRGIHISI NGIAAGLRNT G
//