ID   CAPP_STRPQ              Reviewed;         920 AA.
AC   P0DC99; Q8K873;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-MAY-2023, entry version 44.
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}; OrderedLocusNames=SPs1425;
OS   Streptococcus pyogenes serotype M3 (strain SSI-1).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=193567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSI-1;
RX   PubMed=12799345; DOI=10.1101/gr.1096703;
RA   Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA   Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA   Hattori M., Hamada S.;
RT   "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT   scale genomic rearrangement in invasive strains and new insights into phage
RT   evolution.";
RL   Genome Res. 13:1042-1055(2003).
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=BAC64520.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000034; BAC64520.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P0DC99; -.
DR   SMR; P0DC99; -.
DR   KEGG; sps:SPs1425; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
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.
FT   CHAIN           1..920
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000411437"
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;  104699 MW;  A7837E73861919F7 CRC64;
     MPLKKLESSN NQTIIAEEVA LLKEMLENIT RRMIGDDAFT VIESIMVLSE KQDYIELEKV
     VANISNQEME VISRYFSILP LLINISEDVD LAYEINHQNN TDTDYLGKLA LTIKDLAGKD
     NGKDILEQVN VVPVLTAHPT QVQRKTILEL TTHIHKLLRK YRDAKAGVIN LEKWRQELYR
     YIEMIMQTDI IREKKLQVKN EIKNVMQYYD GSLIQAVTKL TTEYKNLAQK HGLELDNPKP
     ITMGMWIGGD RDGNPFVTAE TLCLSATVQS EVILNYYIDK 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 VADSNTIYRK LVFDNPHFYD
     YFFEASPIKE VSSLNIGSRP AARKTITEIT GLRAIPWVFS WSQNRIMFPG WYGVGSAFKR
     YIDRAQGNLE RLQHMYQTWP FFHSLLSNVD MVLSKSNMNI AFQYAQLAES QDVRDVFYEI
     LDEWQLTKNV ILAIQDHDDL LEDNPSLKHS LKSRLPYFNV LNYIQIELIK RWRNNQLDEN
     DEKLIHTTIN GIATGLRNSG
//