ID   C0MHJ2_STRS7            Unreviewed;       927 AA.
AC   C0MHJ2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   10-JUN-2026, entry version 87.
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   OrderedLocusNames=SZO_12420 {ECO:0000313|EMBL:CAW99736.1};
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483 {ECO:0000313|EMBL:CAW99736.1, ECO:0000313|Proteomes:UP000001368};
RN   [1] {ECO:0000313|EMBL:CAW99736.1, ECO:0000313|Proteomes:UP000001368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70 {ECO:0000313|EMBL:CAW99736.1,
RC   ECO:0000313|Proteomes:UP000001368};
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
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 = phosphoenolpyruvate +
CC         hydrogencarbonate; 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:ARBA00048995, 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; FM204884; CAW99736.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MHJ2; -.
DR   KEGG; seq:SZO_12420; -.
DR   PATRIC; fig|40041.11.peg.1318; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000001368; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   NCBIfam; NF000584; PRK00009.1; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000001368}.
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        590
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   927 AA;  105120 MW;  E2D3E8B7EFDFFB8F CRC64;
     MSVKKLESYN NQEIIAEEVA ILKEILESIT RRMIGDEAFA RIEEIIDLSE KQDYVLLEQL
     IAGISNKDME LISRYFSILP LLINISEDVD LAYEINRQNN TNQDYLGKLA LTIASVAEKE
     NAKELLEKVT VVPVLTAHPT QVQRKTVLEL TNSIHNLLRR YRDVKAGVMN QNKWYSELYR
     YIDILMQTDI IREKKLKVKN EITNVMQYYN SSLIQAITAL TSKYKTLAKD KGILLDNPKP
     INMGMWIGGD RDGNPFVTAE TLRLSATVQS EVILRFYIDK LSALYQTFSL SSALTKTSPE
     VERLASLSSD QSIYRENEPY RRAFHYIQVR LAKTLQELVG QPASDQLASR MPATVGSLQS
     GVTSIVTNSS DQQAPAYKTA AAFKADLVMI EQSLIAAGDS SLVEGDLQEV LQAVDIFGFF
     LASIDLRQDS SVQEACVAEL LKNAGMVENY SALSEEQKCE ILLKELTEDP RTLSSAAVEK
     SELLEKELAI YTAARELKDK LGEEVIKQHI ISHTESVSDM FELAIMLKEV GLIDQRQARV
     QIVPLFETIE DLDNARAIMT QYLSYDIVKS WIATNAGYQE IMLGYSDSNK DGGYLASGWT
     LYKAQNELTK IGEDNDVSIT FFHGRGGTVG RGGGPSYEAI TSQPFGSIKD RIRLTEQGEI
     IENKYGNQDV AYYNLEMLIS ASINRMVTRM LTNPDEIDGF RKIMDEIVED SKRIYRELVF
     DNPHFYDYFF EASPIKEVSS LNIGSRPAAR KTITDISGLR AIPWVFSWSQ NRIMLPGWYA
     VGSAFKRFID KEEGNLAKLQ HMYDKWPFFH SLLSNVDMVL SKSNMNIAFQ YAQLAESKEV
     CEVFHTILDE WQLTKNVILA IAQHDELLEE TPSLKQSLDF RLPYFNVLNY IQIELIKRLR
     HEQLDEDYEK LIHTTINGIA TGLRNSG
//