ID   CAPP_TOLAT              Reviewed;         877 AA.
AC   C4L7S3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Tola_0092;
OS   Tolumonas auensis (strain DSM 9187 / TA4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Tolumonas.
OX   NCBI_TaxID=595494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA   Beller H.;
RT   "Complete sequence of Tolumonas auensis DSM 9187.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; CP001616; ACQ91722.1; -; Genomic_DNA.
DR   RefSeq; WP_012728322.1; NC_012691.1.
DR   AlphaFoldDB; C4L7S3; -.
DR   SMR; C4L7S3; -.
DR   STRING; 595494.Tola_0092; -.
DR   KEGG; tau:Tola_0092; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000009073; 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; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..877
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000212179"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        542
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   877 AA;  100151 MW;  60CCEC8434EA39CC CRC64;
     MNDMYAALRG NVGMLGHLLG KTIKEHLGDE FLDKIENIRQ LAKSSRQGNE EDRQKLITTL
     KNLSDDELLP VARAFSQFLN LANVAEQFHS MSRQGELHTT LDPLDSLFDK LKNANLSEQE
     IIDTVCELDI ELVLTAHPTE VTRRTLIHKH VQLNECLEEL ELQDLTPREC KFIQHRIEQL
     VNQSWHTNEI REQRPTPVDE AKWGFAVIEN NLWPAIPLFL RQLDDRLQEN FGIRLPLRAH
     PVRIASWMGG DRDGNPFVTA KVTQEVLLLS RWVAINLFLT DIQELVSELS MTDCNEELRQ
     RVGECSEPYR AILRVVRDSL RETQQAVTAK LQGQYTENRD LITRTEQLRE PLELCYRSLQ
     SCGMSIIADG MLLDVLRKLA CFGVNLLKLD IRQDGERHGQ VLSELTQYLE LGDYAEWRET
     EKQEFLLKEL ASRRPLLPAN WQPSAESQEV VDTCRVIAQT DPDAFGIYII SMARQPSDVL
     AVQLLLKEVG CKFHMPIAPL FETQNDLQNA AAVLNRLLSV EWYRNYIRGQ QYVMIGYSDS
     AKDAGMMSAG WAQYRAMEDL VAIAEREDLK LTLFHGRGGT IGRGGGPAHQ AILSQPPGSL
     KGGFRVTEQG EMIRFKFGLP EVAIHNFKLY TSAVLEANLL PPPKPEAAWY DVMDKLSEIS
     CQHYRSIVRD EPDFVPYFRA ATPEMELGKL PLGSRPSKRK PNGGVESLRA IPWIFAWTQN
     RLMLPSWLGA HVALQAVMDE GKEDLLKEMD QQWPFFHTRL EMLEMVFLKA DLWLAEYYDL
     RLAPENLWPL GKRLRQELQD SINVVLQLLP KRGELLDDQP WIKESIKLRN PYTDPLNVLQ
     VELLHRSRAT PDEVNPQVDQ ALMVTIAGIA AGMRNTG
//