ID   E6WQA6_PSEUU            Unreviewed;       904 AA.
AC   E6WQA6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
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=Psesu_0497 {ECO:0000313|EMBL:ADV26355.1};
OS   Pseudoxanthomonas suwonensis (strain 11-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV26355.1, ECO:0000313|Proteomes:UP000008632};
RN   [1] {ECO:0000313|EMBL:ADV26355.1, ECO:0000313|Proteomes:UP000008632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL   Submitted (JAN-2011) 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; CP002446; ADV26355.1; -; Genomic_DNA.
DR   RefSeq; WP_013534185.1; NC_014924.1.
DR   AlphaFoldDB; E6WQA6; -.
DR   STRING; 743721.Psesu_0497; -.
DR   KEGG; psu:Psesu_0497; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008632; 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:ADV26355.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008632}.
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   904 AA;  100517 MW;  E9FABE3C577F3B68 CRC64;
     MNAPRNLEFA PPDLPLRDDV RRLGALVGDM LAEQESPAFL EEVEQVRTTA IARRQNGSDI
     QSLAQLLDGL EPAHAQALVR AFSTYFQVVN IAERVHRIRR RRDYQRTGGD TPQPDSLHDA
     LRRLRKAGVE PTELLEWLER VDIEPVFTAH PTEAVRRALL EKEQIMVAAL VDDLDGTRTP
     GERAADLARF RMALTSTWQT ADSSPVRPTV DDEREHVGFY LTEVLYRIMP AFYETLEHAL
     GESFGIASEL PRLLRFGTWV GGDMDGNPNV DATTIRNTLD AQRRAILGKY AAELQQLASV
     LTQSTGVAGV DEAVFERLEQ YRALLPQAAA SSRPRHADMP YRLLLELMRA RLLATLEDQA
     VGYGSPDEFA QDLDLVRKSL EHNRGVHAGW FSVRRLVWRL RTFGFHLARL DVRQESTVHA
     RAIAAALGDE QWEGRDPVEQ AGILAGHAGE GEPLPQAGDE GNKRLDAVFQ ALGDARRRHG
     ADALGAYIIS MARSRADVLA VLALARRGGL VDEAGRVPLD IAPLFETVDD LHHGPDTLRD
     LFADPVYREH LQARGNVQMV MLGYSDSGKD GGIAASRWSL QRAQVELLQV AEEHGIRLTF
     FHGRGGSLSR GGSKTTRAVD ASPRGSVDGR LRVTEQGEAI HRKFGIRALA LRSLEQTTGA
     VLVSSIRPRP PEPREARWRE VMDTVAEASS VAYRALVGAP RFMDYFRSAT PIDVIERMTL
     GSRPSRRLGQ DAALSNLRAI PWVFAWSQAR AVIPGWYGVG SGLQAAAEQH GEEVLREMAA
     DWPFFRTFLD DLAMVLAKGD MGIAEMFSRL SGDELHGEFF PRISDEHAHT RQWLLRLNGH
     EFLLQHDQRL ALSIRLRNPY VDPISVLQAD LLRRWRASGR EDDDLLRALV ASVNGVSQGV
     QNTG
//