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Database: UniProt
Entry: W5XYU6_9CORY
LinkDB: W5XYU6_9CORY
Original site: W5XYU6_9CORY 
ID   W5XYU6_9CORY            Unreviewed;       868 AA.
AC   W5XYU6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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   ORFNames=B843_04010 {ECO:0000313|EMBL:AHI22191.1};
OS   Corynebacterium vitaeruminis DSM 20294.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1224164 {ECO:0000313|EMBL:AHI22191.1, ECO:0000313|Proteomes:UP000019222};
RN   [1] {ECO:0000313|EMBL:AHI22191.1, ECO:0000313|Proteomes:UP000019222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10234 {ECO:0000313|Proteomes:UP000019222};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "The complete genome sequence of Corynebacterium vitaeruminis DSM 20294.";
RL   Submitted (FEB-2013) 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,
CC         ECO:0000256|HAMAP-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; CP004353; AHI22191.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5XYU6; -.
DR   STRING; 1224164.B843_04010; -.
DR   KEGG; cvt:B843_04010; -.
DR   PATRIC; fig|1224164.3.peg.795; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000019222; 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:AHI22191.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019222}.
FT   ACT_SITE        114
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        532
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   868 AA;  96890 MW;  7F4066BFCBEEB1B0 CRC64;
     MLGRVIAQQE GEDVFELVEA TRRMAFDIAH GDAKPTDLMG IFRDLDITKT NLVARSFCYF
     ALIANLAEDL ADESVEAPVS LRKTFAKLKD AGVTGADAAA VVRNAKVAPV LTAHPTETRR
     RTVFDTQNRI KQLLKESHHG GDMARIEREM YLRITLLWQT ALIRIARPTL EDEVDVGLRY
     YKLSLLEQVP ALNRAIRHNM RDTFGMQVPD VPVVRPGSWI GGDHDGNPYV NARTLTYATR
     NAAKTVLRFY EEQLGELERE LSLSDRYSSC SKELLALADA AHNDWESRVD EPYRRAIYGI
     RNRVRANLHE IGDKKVAQVD AAAYASPEEF KRDLDTIDRS LRQFNDDVIA DDRLARIRSA
     VTTFGFHLYT LDLRQNSESF ENVLTEVFAA AGRSDDYRAL GEEEKIALLV EELKTPRPLL
     FPDAAPMSEV TEKELGIFRA AAQAVRNFGP QSVSHCIISM TGTVSDILEP MVLLKEVGLR
     EVDVVPLFET IDDLKAGAGI LEKLWSVPFY REHLRARGDV QEVMLGYSDS NKDGGYLQAN
     WALYDAELAL VELCNAHGIE LRLAHGRGGA VGRGGGPTYD AILAQPKGAV SGSVRITEQG
     EVISAKYGAP ETARRHLEAF VSGALVASLT DTEPIADPDR AYAIMRELSD LSGQKYQELV
     GDPGFIEYFT QSTPLHEIGD LNLGSRPAAR KQTTAISDLR AIPWVLSWSQ SRTNVPGWFG
     VGSAVTRWAG EDASRWEELR ALHRDWPFFR SVMSNMAQVM AKAEISLARL YANLVDDKQI
     ADRIYTLIAE EFELTKKVYL EVTGNKDLTA ENQRQARSLK RRYPYLLPLN AIQLELLRRY
     RAGDDSFLVS KTIQVTMNGL ATALRNAG
//
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