ID   C3PLB5_CORA7            Unreviewed;       884 AA.
AC   C3PLB5;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 84.
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:ACP32119.1};
GN   OrderedLocusNames=cauri_0522 {ECO:0000313|EMBL:ACP32119.1};
OS   Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS   CN-1) (Corynebacterium nigricans).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=548476 {ECO:0000313|EMBL:ACP32119.1, ECO:0000313|Proteomes:UP000002077};
RN   [1] {ECO:0000313|EMBL:ACP32119.1, ECO:0000313|Proteomes:UP000002077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1
RC   {ECO:0000313|Proteomes:UP000002077};
RX   PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA   Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA   Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA   Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT   "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT   aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT   vaginal swab of a woman with spontaneous abortion.";
RL   BMC Genomics 11:91-91(2010).
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; CP001601; ACP32119.1; -; Genomic_DNA.
DR   RefSeq; WP_010189403.1; NZ_ACLH01000061.1.
DR   AlphaFoldDB; C3PLB5; -.
DR   STRING; 548476.cauri_0522; -.
DR   GeneID; 31923141; -.
DR   KEGG; car:cauri_0522; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002077; 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:ACP32119.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002077}.
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   884 AA;  98875 MW;  EEA2440586877A9A CRC64;
     MSTPAPEQVR EDIRFLGRVL GRVIAQQEGE DVFELVESTR RMAFDIAHGD AKPEDLVAIF
     RDLDITKVNL VARAFSYFAL IANLAEDLDD ESVEAPVSLR KTFAKLKEEG VAPADAASVI
     RGAHVAPVLT AHPTETRRRT VFDTQTRIKT LLKESHRGGD MAAIEKEMYL RMTLLWQTAL
     IRIARPTLED EIDVGLRYYK LSLLDQVPAL NRAIRHAMRE TFGQQLPDSP VVRPGSWIGG
     DHDGNPFVNE HTLTYATRKA AATVLQYYAD ELGELERELS LSDRYSSSSK ELGALADASH
     NDEKSRVDEP YRRAIFGIRK KVLARLEGEA SPSAYASPEE LKRDLDVIDR SLRQFNDDII
     ADDRLARLRS AVTTFGFHLS TLDMRQNSES FENVLTEIFA AARITPDYRA LGEEEKVALL
     VRELQTNRPL LFPGTEKEFT EDTAKELGIF RAAARAVRDF GPKSVSHCII SMTGTVSDIL
     EPMVLLKEVG LGQVDVVPLF ETIEDLKAGA SILEKLWQMP VYREHLRSRG DVQEVMLGYS
     DSNKDGGYLQ ANWALYDAEL ALVELCVRHG VELRLAHGRG GAVGRGGGPT YDAILAQPKG
     AVSGSVRITE QGEVISAKYG APETARRHLE AFISGALEAS LLDTEPIADP ERAYEIMREL
     ADLSGTAYRQ LVDDPGFIAY FTQSTPLHEI GELNLGSRPT SRKQTTAITD LRAIPWVLSW
     SQSRTNIPGW FGVGSAVTAW VQQAGGDEEK RWEELRELYR TWPFFRSVFA NMAQVMAKAE
     MQLARLYANL VDDKETADRI FGLISVEFER TREVYLKVTG NADLVSENQR QARSLKRRYP
     YLLPLNAIQL ELLRRYRRGD DQFLVSKTIQ VTMNGLATAL RNAG
//