ID   CAPP_STRP8              Reviewed;         920 AA.
AC   Q8P1W7;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; Synonyms=pepC;
GN   OrderedLocusNames=spyM18_0675;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; AE009949; AAL97351.1; -; Genomic_DNA.
DR   RefSeq; WP_011017539.1; NC_003485.1.
DR   AlphaFoldDB; Q8P1W7; -.
DR   SMR; Q8P1W7; -.
DR   KEGG; spm:spyM18_0675; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   OMA; PWVFGWT; -.
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_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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium.
FT   CHAIN           1..920
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166635"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        583
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   920 AA;  104481 MW;  6AD6E50E0DF929C1 CRC64;
     MPLKKLESSN NQAIIAEEVA LLKEMLENIT RRMIGDDAFT VIESIMVLSE KQDYIELEKV
     VANISNQEME VISRYFSILP LLINISEDVD LAYEINYQNN TDTDYLGKLA LTIKDLAGKD
     NGKDILEQVN VVPVLTAHPT QVQRKTILEL TTHIHKLLRK YRDAKAGVIS LEKWRQELYR
     YVEMIMQTDI IREKKLQVKN EIKNVMQYYD GSLIQAVTKL TTEYKNLAQK HGLELDNPKP
     ITMGMWIGGD RDGNPFVTAE TLCLSATVQS EVILNYYIDK LAALYRTFSL SSTLVQPNSE
     VERLASLSQD QSIYRGNEPY RRAFHYIQSC LKQTQIQLTN QPAARMSSSV GLNTSACPSP
     ASLENPILAY DSPVDFKADL KAIEQSLLDN GNSALIEGDL REVMQAVDIF GFFLASIDMR
     QDSSVQEACV AELLKGANIV DDYSSLSETE KCDVLVQQLM EEPRTLSSAA VAKSDLLEKE
     LAIYTTAREL KDKLGEEVIK QHIISHTESV SDMFELAIML KEVGLVDQQR ARVQIVPLFE
     TIEDLDNACD IMAAYLSHDI VKSWIATNRN YQEIMLGYSD SNKDGGYLAS GWTLYKAQNE
     LTAIGEEHGV KITFFHGRGG TVGRGGGPSY DAITSQPFGS IKDRIRLTEQ GEIIENKYGN
     KDVAYYHLEM LISASINRMV TQMITDSNEI DSFREIMDSI VADSNMIYRK LVFDNPHFYD
     YFFEASPIKE VSSLNIGSRP AARKTITEIT GLRAIPWVFS WSQNRIMFPG WYGVGSAFKR
     YIDRAQGNLE RLQHMYQTWP FFHSLLSNVD MVLSKSNMNI AFQYAQLAES QDVRDVFYEI
     LDEWQLTKNV ILAIQDHDDL LEDNPSLKHS LKSRLPYFNV LNYIQIELIK RWRNNQLDEN
     DEKLIHTTIN GIATGLRNSG