ID   CAPP_STRP1              Reviewed;         920 AA.
AC   Q9A0U7; Q48ZU5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 2.
DT   24-JAN-2024, entry version 134.
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};
GN   OrderedLocusNames=SPy_0608, M5005_Spy0505;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   SEQUENCE REVISION TO 345.
RA   Beres S.B., Musser J.M.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ51123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004092; AAK33584.2; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51123.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_268863.2; NC_002737.2.
DR   AlphaFoldDB; Q9A0U7; -.
DR   SMR; Q9A0U7; -.
DR   PaxDb; 1314-HKU360_00517; -.
DR   KEGG; spy:SPy_0608; -.
DR   KEGG; spz:M5005_Spy0505; -.
DR   PATRIC; fig|160490.10.peg.520; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000000750; 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; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..920
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166632"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        583
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   CONFLICT        859
FT                   /note="D -> A (in Ref. 3; AAZ51123)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   920 AA;  104821 MW;  080B1F5D4C199237 CRC64;
     MPLKKLESSN NQDIIAEEVA LLKEMLENIT RRMIGDDAFT VIESIMVLSE KQDYIELEKV
     VANISNQEME VISRYFSILP LLINISEDVD LAYEINYQNN TDTDYLGKLA LTIKDLAGKD
     NGKDILEQVN VVPVLTAHPT QVQRKTILEL TTHIHKLLRK YRDAKAGVIN LEKWRQELYR
     YIEMIMQTDI IREKKLQVKN EIKNVMQYYD GSLIQAVTKL TTEYKNLAQK HGLELDNPKP
     ITMGMWIGGD RDGNPFVTAE TLCLSATVQS EVILNYYIDE LAALYRTFSL SSTLVQPNSE
     VERLASLSQD QSIYRGNEPY RRAFHYIQSR LKQTQIQLTN QPAARMSSSV GLNTSAWSSP
     ASLENPILAY DSPVDFKADL KAIEQSLLDN GNSALIEGDL REVMQAVDIF GFFLASIDMR
     QDSSVQEACV AELLKGANIV DDYSSLSETE KCDVLLQQLM EEPRTLSSAA VAKSDLLEKE
     LAIYTTAREL KDKLGEEVIK QHIISHTESV SDMFELAIML KEVGLVDQQR ARVQIVPLFE
     TIEDLDNARD IMAAYLSHDI VKSWIATNRN YQEIMLGYSD SNKDGGYLAS GWTLYKAQNE
     LTAIGEEHGV KITFFHGRGG TVGRGGGPSY DAITSQPFGS IKDRIRLTEQ GEIIENKYGN
     KDVAYYHLEM LISASINRMV TQMITDPNEI DSFREIMDSI VADSNIIYRK LVFDNPHFYD
     YFFEASPIKE VSSLNIGSRP AARKTITEIT GLRAIPWVFS WSQNRIMFPG WYGVGSAFKR
     YIDRAQGNLE RLQHMYQTWP FFHSLLSNVD MVLSKSNMNI AFQYAQLAER QDVRDVFYEI
     LDEWQLTKNV ILAIQDHDDL LEDNPSLKHS LKSRLPYFNV LNYIQIELIK RWRNNQLDEN
     DEKLIHTTIN GIATGLRNSG
//