ID   CAPP_STRMU              Reviewed;         907 AA.
AC   Q8DV10;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=capP;
GN   OrderedLocusNames=SMU_712;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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; AE014133; AAN58441.1; -; Genomic_DNA.
DR   RefSeq; NP_721135.1; NC_004350.2.
DR   RefSeq; WP_002263316.1; NC_004350.2.
DR   AlphaFoldDB; Q8DV10; -.
DR   SMR; Q8DV10; -.
DR   STRING; 210007.SMU_712; -.
DR   KEGG; smu:SMU_712; -.
DR   PATRIC; fig|210007.7.peg.631; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   OrthoDB; 9768133at2; -.
DR   PhylomeDB; Q8DV10; -.
DR   Proteomes; UP000002512; 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..907
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166629"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        570
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   907 AA;  103896 MW;  286DAB90F19FBE8C CRC64;
     MTINKLESRN DKEAIAEEIT ILTKLLDDAT KTMVGSASFD KITLFKKLSI EEKHQELERE
     IEQLTNEEMV VVSRYFSILP LLINISEDVN LAYEINYQNN NDIDYLGKLS ATIELVSSQK
     NAQEILENVN VVPVLTAHPT QVQRKTMLDL TNHIHELLRK YRDVKAGSIN KQKWYDDMRR
     YVELIMQTDI IREKKLKVTN EITNVMEYYN SSLIKGVTKL ITEYKHLSHQ KGFDLGNAKP
     ITMGMWIGGD RDGNPFVTAE TLKISALVQN EVILNYYIDK VSDLYRTFSL STSLSTISNA
     VKEMADRSTD VSIYREKEPY RKAFHYIQSR LQETLIYLKN NHLEELESED SAQILPYQSA
     QEFRNDLQLI KDSLLENNGS AFITGDLTEL LQAVDVFGFF LASIDMRQDS SVHETCVAEL
     LASANIVANY SDLPEEEKIA ILLKELTEDP RILSATHVEK SEILQKELAI FKTARKLKDA
     LGEDVIKQHI ISHTESISDM FELAIMLKEV GLVDTDKARV QIVPLFETIE DLDNSREIMR
     QYLNYDIVKK WIAANHNYQE IMLGYSDSNK DGGYLSSGWA LYKAQNELTE IGYDNGVKIT
     FFHGRGGTVG RGGGPSYEAI TSQPFGSIKD RIRLTEQGEV IGNKYGNKDV AYYNLEMLVS
     ATLDRMVTRR IVNSDNLVNY RLIMDEIVAD SNLIYRDLVF GNEHFYDYFF AASPIREVSS
     LNIGSRPAAR KTITEISGLR AIPWVFSWSQ NRIMFPGWYG VGSAFKHFID KDEKNLTKLQ
     EMYQSWPFFH SLLSNVDMVL SKSNMNIAFE YAKLCQDEET KEVFATILDE WQLTKNVILA
     IESHKQLLED NSYLKASLDY RLPYFNVLNY IQIELIKRQR RGELGENLEN LIHITINGVA
     TGLRNSG
//