ID   G7UPR7_PSEUP            Unreviewed;       903 AA.
AC   G7UPR7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
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=DSC_04770 {ECO:0000313|EMBL:AER55607.1};
OS   Pseudoxanthomonas spadix (strain BD-a59).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER55607.1, ECO:0000313|Proteomes:UP000005870};
RN   [1] {ECO:0000313|EMBL:AER55607.1, ECO:0000313|Proteomes:UP000005870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD-a59 {ECO:0000313|EMBL:AER55607.1,
RC   ECO:0000313|Proteomes:UP000005870};
RX   PubMed=22207748; DOI=10.1128/JB.06436-11;
RA   Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT   "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT   spadix BD-a59.";
RL   J. Bacteriol. 194:544-544(2012).
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; CP003093; AER55607.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7UPR7; -.
DR   STRING; 1045855.DSC_04770; -.
DR   KEGG; psd:DSC_04770; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000005870; 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:AER55607.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005870}.
FT   ACT_SITE        150
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        569
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   903 AA;  99239 MW;  D71F3C2DB6E1E84C CRC64;
     MSASSPVSEY AAPDLPLRDD VRRLGAVVGD MLAEQVSPEF LDRVEAIRTA AIARRQKGES
     TQGLAQTLAG MPAGDAQALI RAFSAYFQVV NIAERVHRIR RRRDYQRQGD APQPEGLHAS
     LLKLRAQGVD LAEASAWLER IDLEPVFTAH PTEAVRRALL EKEQLMVASL VAGLDKVRTP
     GEAAADAARF RMALTAAWQT ADSSPVRPTV DDEREHVGFY LTEVLYRVIP VFYESLEHAF
     TATYGSAPEL PRVLRFGTWV GGDMDGNPNV DAGTIAATLR AQRHAIVHRY QAELKALGSL
     LSQSTQLVQV SPEVLRRVDQ YRALLPEAAA RARPRHADMP YRLLLDLMRA RLHATLDEQD
     RGYAGPEAFG QDVALILHSL EANRGVHAGW FAVRRLAWRV RTFGFHLARL DVRQESGVHA
     RALAAALGDA GFEARDASAR AALLQPYAAG EQLLPASTEE GNSRLDAVFA ALSQARRLHG
     ADALGAYIIS MAHSRADVLT VLALARRGGL VDDQGQVPLD IAPLFETVED LRHGPEVLRE
     LATDPVYRRH LAARGDTQMV MLGYSDSGKD GGTTASRWGL QRGQVELLET AHALGIRLTF
     FHGRGGSISR GGGKTTRAVD ASPRGSVDGR LRVTEQGEVI HRKYGIRALA VRSLEQSLGA
     VLVSSIRPRP PEPREAQWRR IMDTVSRASN RAYRDFVGAP GFMDYFRSAT PIDVIERMTL
     GSRPSRRLGQ DAALDNLRAI PWVFAWSQAR ATIPGWYGVG SGLAAAVDEF GEDAVREMGR
     DWPFVRTFLD DIAMVLAKGD LDIAALFSQL SGELHGRFFP LIQAEHALTR QWLLRLNGSD
     TLLQHDQRLD LSIRLRNPYV DPMSLLQVDL LRRWRAAGRE DEGLLRALVA SVNGVSQGVQ
     NTG
//