ID   A4QEF9_CORGB            Unreviewed;       920 AA.
AC   A4QEF9;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=cgR_1633 {ECO:0000313|EMBL:BAF54625.1};
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=340322 {ECO:0000313|EMBL:BAF54625.1, ECO:0000313|Proteomes:UP000006698};
RN   [1] {ECO:0000313|Proteomes:UP000006698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R {ECO:0000313|Proteomes:UP000006698};
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
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; AP009044; BAF54625.1; -; Genomic_DNA.
DR   RefSeq; WP_011897300.1; NC_009342.1.
DR   AlphaFoldDB; A4QEF9; -.
DR   KEGG; cgt:cgR_1633; -.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   PhylomeDB; A4QEF9; -.
DR   Proteomes; UP000006698; 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}.
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        580
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   920 AA;  103441 MW;  265DDAF048E2E398 CRC64;
     MTDFLRDDIR FLGRILGEVI AEQEGQEVYE LVEQARLTSF DIAKGNAEMD SLVQVFDGIT
     PAKATPIARA FSHFALLANL AEDLHDEELR EQALDAGDTP PDSTLDATWL KLNEGNVGAE
     AVADVLRNAE VAPVLTAHPT ETRRRTVFDA QKWITTHMRE RHALQSAEPT ARTQSKLDEI
     EKNIRRRITI LWQTALIRVA RPRIEDEIEV GLRYYKLSLL EEIPRINRDV AVELRERFGE
     DVPLKPVVKP GSWIGGDHDG NPYVTAETVE YSTHRAAETV LKYYARQLHS LEHELSLSDR
     MNKVTPQLLA LADAGHNDVP SRVDEPYRRA VHGVRGRILA TTAELIGEDA VEGVWFKVFT
     PYASPEEFLN DALTIDHSLR ESNDTLIADD RLSVLISAIE SFGFNLYSLD LRQNSESYED
     VLTELFERAQ VTANYRELSE EEKLEVLLKE LRSPRPLIPH GSDEYSEVTD RELGIFRTAS
     EAVKKFGPRM VPHCIISMAS SVTDVLEPMV LLLKEFGLIA ANGDNPRGTV DVIPLFETIE
     DLRAGAGILG ELWKIDLYRN YLLQRDNVQE VMLGYSDSNK DGGYFSANWA LYDAELQLVE
     LCRSAGVKLR LFHGRGGTVG RGGGPSYDAI LAQPKGAVQG SVRITEQGEI ISAKYGNPET
     ARRNLEALVS ATLEASLLDV SELTDHQRAY DIMSEISELS LKKYTSLVHE DQGFIDYFTQ
     STPLQEIGSL NIGSRPSSRK QTSSVEDLRA IPWVLSWSQS RVMLPGWFGV GTALEQWIGE
     GEQATQRIAE LQTLNESWPF FTSVLDNMAQ VMSKAELRLA KLYADLIPDR EVAERVYSVI
     HEEYFLTKKM FCVITGSDDL LDDNPLLARS VQRRYPYLLP LNVIQVEMMR RYRKGDQSEQ
     VSRNIQLTMN GLSTALRNSG
//