ID   CAPP_COREF              Reviewed;         919 AA.
AC   Q8RQL3;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
GN   Name=ppc; OrderedLocusNames=CE1703;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RA   Akiyoshi N., Nonaka G., Kimura E., Kawahara Y., Sugimoto S.;
RT   "Corynebacterium efficiens ppc gene for phosphoenolpyruvate carboxylase,
RT   complete CDS.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; AB083298; BAB88902.1; -; Genomic_DNA.
DR   EMBL; BA000035; BAC18513.1; -; Genomic_DNA.
DR   RefSeq; WP_006767704.1; NZ_GG700683.1.
DR   AlphaFoldDB; Q8RQL3; -.
DR   SMR; Q8RQL3; -.
DR   STRING; 196164.23493543; -.
DR   EnsemblBacteria; BAC18513; BAC18513; BAC18513.
DR   KEGG; cef:CE1703; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   Proteomes; UP000001409; 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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 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..919
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166590"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        579
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   919 AA;  103096 MW;  E2D8FE8DD5BC6E51 CRC64;
     MNELLRDDIR YLGRILGEVI SEQEGHHVFE LVERARRTSF DIAKGRAEMD SLVEVFAGID
     PEDATPVARA FTHFALLANL AEDLHDAAQR EQALNSGEPA PDSTLEATWV KLDDAGVGSG
     EVAAVIRNAL VAPVLTAHPT ETRRRTVFDA QKHITALMEE RHLLLALPTH ARTQSKLDDI
     ERNIRRRITI LWQTALIRVA RPRIEDEVEV GLRYYKLSLL AEIPRINHDV TVELARRFGG
     DIPTTAMVRP GSWIGGDHDG NPFVTAETVT YATHRAAETV LKYYVKQLHA LEHELSLSDR
     MNVISDELRV LADAGQNDMP SRVDEPYRRA IHGMRGRMLA TTAALIGEEA VEGTWFKTFT
     PYTDTHEFKR DLDIVDGSLR MSRDDIIADD RLAMLRSALD SFGFNLYSLD LRQNSDGFED
     VLTELFATAQ TEKNYRGLTE AEKLDLLIRE LSTPRPLIPH GDPDYSEATN RELGIFSKAA
     EAVRKFGPLM VPHCIISMAS SVTDILEPMV LLKEFGLIRA NGKNPTGSVD VIPLFETIDD
     LQRGAGILEE LWDIDLYRNY LEQRDNVQEV MLGYSDSNKD GGYFAANWAL YDAELRLVEL
     CRGRNVKLRL FHGRGGTVGR GGGPSYDAIL AQPKGAVRGA VRVTEQGEII SAKYGNPDTA
     RRNLEALVSA TLEASLLDDV ELPNRERAHQ IMGEISELSF RRYSSLVHED PGFIQYFTQS
     TPLQEIGSLN IGSRPSSRKQ TNTVEDLRAI PWVLSWSQSR VMLPGWFGVG TALREWIGEG
     EGAAERIAEL QELNRCWPFF TSVLDNMAQV MSKAELRLAR LYADLIPDRE VADRIYETIF
     GEYFLTKEMF CTITGSQDLL DDNPALARSV RSRFPYLLPL NVIQVEMMRR YRSGDEGTAV
     PRNIRLTMNG LSTALRNSG