ID   G0HDF8_CORVD            Unreviewed;       946 AA.
AC   G0HDF8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
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   ECO:0000313|EMBL:AEK36832.1};
GN   OrderedLocusNames=CVAR_1480 {ECO:0000313|EMBL:AEK36832.1};
OS   Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS   NCIMB 30131) (Corynebacterium mooreparkense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK36832.1, ECO:0000313|Proteomes:UP000006659};
RN   [1] {ECO:0000313|EMBL:AEK36832.1, ECO:0000313|Proteomes:UP000006659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC   {ECO:0000313|Proteomes:UP000006659};
RX   PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA   Schroeder J., Maus I., Trost E., Tauch A.;
RT   "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT   from the surface of smear-ripened cheeses and insights into cheese ripening
RT   and flavor generation.";
RL   BMC Genomics 12:545-545(2011).
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; CP002917; AEK36832.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0HDF8; -.
DR   STRING; 858619.CVAR_1480; -.
DR   KEGG; cva:CVAR_1480; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000006659; 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:AEK36832.1}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        609
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   946 AA;  103731 MW;  8E385AFD9E2B1520 CRC64;
     MTESSPETPP RQSVPGTAVP VVPPDVDTPE IIPGVRQDIR YLGAILGDII REQEGQEVFD
     LVESARRAAF GIRQGDGTVE VLATRLRDLP ADRALPVIRA FSHFSLLANL AEDLHEERVR
     DRLADAGDPP PASTLAATWP TLTEGGVTSG EVAEVMGRAH VAPVLTAHPT ETRRRTVFDV
     QSDITRLMRS RGRIIAAGLT ARSDERLAEI DRDIRRRVTI LWQTALIRSV RPRIEDEINV
     GLRYFTISLL HEIPLLNLRV SNALREQFGP GVPDTPVVRP GSWIGGDHDG NPFVTGDTVR
     YATHRAAQTV FSWYLAELAE LEHELSLSTR FTVVEPELDD LADRGHNDVP SRSDEPYRRA
     VHGIRGRIAA AAVATLGAGS VVPGVADGHT PYPDAATALE DLAVIDRSLR ASNDGIIADH
     RLATVITALR TFGFHLSALD LRQNSESFEN VLTEILARAG VADDYSSLTE EEKILLLTRE
     LHSPRPLVDP LAEWSEATGR ELGIFRSAAD AARRFGPEVV PHCIISMASS VSDILEPVLL
     LKEVGLVRVE DGVLHGSVDV IPLFETIDDL KAGASVMTEL WSHDFYRTYV AEEREGIQEV
     MLGYSDSNKD GGYFAANWAL YDAELALVDT SRAAGLGLRL FHGRGGTVGR GGGPSHEAIL
     AQPEGAVQGS VRITEQGEII SAKYGVRSVA RRNLEALVSA TLEASLLPVD RVEEPEKAYA
     TMRELSELSR KTYSALMHED PGFIGYFTSS TPLAEIGNLN IGSRPSSRKQ TSSISDLRAI
     PWVLSWSQSR IMLPGWYGVG SALSAWVGED AERLAFLRKL HREWPFFRSV MSNMAQVMAK
     ADLAVAKMYA GLVPDRADAD RIFEAIVKEF HLTLDMYVKV TGTESLLDDN PELAVSMRNR
     FPYLIPLNLI QLELLRRYRA GDESEDVLDG IRLTMNGLAT GLRNSG
//