ID   CAPP_STRSV              Reviewed;         948 AA.
AC   A3CP10;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=SSA_1521;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN44915.1; -; Genomic_DNA.
DR   RefSeq; WP_011837193.1; NC_009009.1.
DR   RefSeq; YP_001035465.1; NC_009009.1.
DR   AlphaFoldDB; A3CP10; -.
DR   SMR; A3CP10; -.
DR   STRING; 388919.SSA_1521; -.
DR   PRIDE; A3CP10; -.
DR   EnsemblBacteria; ABN44915; ABN44915; SSA_1521.
DR   KEGG; ssa:SSA_1521; -.
DR   PATRIC; fig|388919.9.peg.1445; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   Proteomes; UP000002148; 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   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; Reference proteome.
FT   CHAIN           1..948
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025596"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        610
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   948 AA;  108729 MW;  3844FEDF343B17C5 CRC64;
     MSFNKLESYS NKEVIREEVA ILTDLLADIT RNLLSPETFE KISLMEDLAV NSKYHELKAI
     VEELTTDEMV YISRYFSILP LLINISEDVD LAYEINHQNN INQDYLGKLS TTIDLISTRE
     NAQEILENLN VVPVLTAHPT QVQRKTILDL TNHIHSLLRQ HRDVKAGLVN EKKWLGNLRR
     YIELMMQTDM IREKKLKVTN EITNVMEYYN SSFLQAITNF MVEYRRLAEE RGIKLDNPKP
     ITMGMWIGGD RDGNPFVTAE TLKLSATLQS EVILNYYIDK VYTLYRTFSL STNLSETSQA
     VAEMAALSTD KSVYRENEPY RRAFHYIQSK LIQTLLYLKE GNFSNDGQRL TDRAEEKLSA
     KANLSVSNKG REIIPNYIQS RISETLTELK KEETPSYKTA QEFKEDLQVI YDSLIEHHGE
     ALVSGDLTEL LQAVDVFGFF LASIDMRQDS SVHEACVAEL LASANIVQDY SSLSEEEKCQ
     VLLKQLLEDP RILSATHEPK SELLQKELEI FKTARQLKDA IGEEVIKQNI ISHSTSVSDL
     LELAIMLKEV GLIDENGARV QIVPLFETIE DLDNSCNTME KYLSLPIAQK WIASKDNYQE
     IMLGYSDSNK DGGYLSSCWT LYKAQQQLTA IGDKFGVKIT FFHGRGGTVG RGGGPTYEAI
     TSQPLRSIND RIRLTEQGEV IGNKYGNKDA AYYNLEMLVS AAINRMVTHK KSDSHTSDKY
     ERIMDQVVNR SYQIYRDLVF GDERFYDYFF ESSPIKAISS FNIGSRPAAR KTITEIGGLR
     AIPWVFSWSQ SRVMFPGWYG VGSSFKEFID EDPENNLAFL QFMYKRWPFF KSLLSNVDMV
     LSKSNMNIAF EYAQLCEDQN VRDIFNIILD EWQLTKDVIL EIEGHDELLA ENTYLRDSLH
     YRMPYFNVLN YIQLELIKRQ RNGQLTPDQE KLIHITINGI ATGLRNSG