ID   CAPPA_CLOP1             Reviewed;         537 AA.
AC   Q0TRE4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_01904};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_01904};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_01904};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_01904};
GN   Name=ppcA {ECO:0000255|HAMAP-Rule:MF_01904};
GN   OrderedLocusNames=CPF_1350;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S
RC   107 / Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
CC   -!- FUNCTION: Catalyzes the irreversible beta-carboxylation of
CC       phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon
CC       dicarboxylic acid source for the tricarboxylic acid cycle.
CC       {ECO:0000255|HAMAP-Rule:MF_01904}.
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:0000255|HAMAP-Rule:MF_01904};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01904};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01904}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01904}.
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DR   EMBL; CP000246; ABG83743.1; -; Genomic_DNA.
DR   RefSeq; WP_011590671.1; NC_008261.1.
DR   AlphaFoldDB; Q0TRE4; -.
DR   SMR; Q0TRE4; -.
DR   STRING; 195103.CPF_1350; -.
DR   PaxDb; 195103-CPF_1350; -.
DR   KEGG; cpf:CPF_1350; -.
DR   eggNOG; COG1892; Bacteria.
DR   HOGENOM; CLU_517433_0_0_9; -.
DR   Proteomes; UP000001823; 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_01904; PEPcase_type2; 1.
DR   InterPro; IPR007566; PEP_COase_arc-type.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   NCBIfam; TIGR02751; PEPCase_arch; 1.
DR   Pfam; PF14010; PEPcase_2; 1.
DR   PIRSF; PIRSF006677; UCP006677; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium.
FT   CHAIN           1..537
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000309594"
SQ   SEQUENCE   537 AA;  60393 MW;  CF43D5B22E28014C CRC64;
     MKIPCSMMTQ HPDNVETYIS IQQEPAEAIK GLTPQDKGGL GIEEVMIDFE GKLTPYHQTS
     QIALGLISNG IIPGKDVRVT PRIPNANKES VFRQLMSIMS IIETNVQSKE LTGIPAISEV
     VVPMIETGKE ISEFQDRVNS VVDMGNKNYK TKLDLNSVRI IPLVEDVPAL ANIDRILDEH
     YEIEKSKGHV LKDLRIMIAR SDTAMSYGLI SGVLSVLMAV DGAYKWGEKH GVTISPILGC
     GSLPFRGHFS EENIDEILAT YSGIKTFTFQ SALRYDHGEE ATKHAVNELK AKIAESKPRN
     FSEEDKDLMK EFIGICSKHY LQTFLKVIDT VSFVSDFIPK NRDRLTKAKT GLEYNREVAN
     LDNVADLVKD EVLKQEILSI DNSKEYAVPR AISFTGAMYT LGMPPELMGM GRALNEIKTK
     YGQEGIDKLL EIYPILRKDL AFAARFANGG VSKKIIDEEA RQEYKEDMKY VNEILNLGLD
     YDFLNENEFY HTLLKTTKPI IMHLMGLEEN VMRNSTEELK ILNEWIVRMG KVRGSIG
//