ID   CAPP_STRGC              Reviewed;         948 AA.
AC   A8AW99;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=SGO_0760;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(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; CP000725; ABV09428.1; -; Genomic_DNA.
DR   RefSeq; WP_012000224.1; NC_009785.1.
DR   AlphaFoldDB; A8AW99; -.
DR   SMR; A8AW99; -.
DR   STRING; 467705.SGO_0760; -.
DR   PRIDE; A8AW99; -.
DR   EnsemblBacteria; ABV09428; ABV09428; SGO_0760.
DR   KEGG; sgo:SGO_0760; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000001131; 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_1000082437"
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;  108837 MW;  6E585C733AC2DC54 CRC64;
     MSFNKLESFS NKEVIREEVS ILTDLLTDVT RKILSPETFE KIAMMEDLAV HSKYQELKEI
     VEELTTEEMV YISRYFSILP LLINISEDVD LAYEINHQNN IDQDYLGKLS TTIDLISTRE
     NAKEILENLN VVPVLTAHPT QVQRKTMLDL TNHIHTLLRQ HRDVKAGLVN EKKWLGNLRR
     YIELMMQTDM IRDKKLKVTN EITNVMEYYN SSFLQAITNF MVEYKRLAEE RGIKLDNPKP
     ITMGMWIGGD RDGNPFVTAE TLKLSATLQS EVILNYYIDK VYTLYRTFSL STNLSETSQA
     VAEMAALSTD KSVYRENEPY RRAFHYIQSK LIQTLLYLKE GNFSNEGQRL TDRAEKTLSA
     KTTPSLSNKG REIIPNYIQS RISETLTELK KEETPSYKTA KEFKEDLQVI YDSLIEHHGE
     ALVTGDLTEL LQAVDVFGFF LASIDMRQDS SVHEACVAEL LASANIVKDY SSLSEEEKCQ
     VLLKQLLEDP RILSATHEPK SELLQKELEI FKTARQLKDA LGEEVIKQNI ISHSTSVSDL
     LELAIMLKEV GLIDENGTRV QIVPLFETIE DLDNSCETME KYLSLPIAQK WIASKNNYQE
     IMLGYSDSNK DGGYLSSCWT LYKAQQQLTA IGDKFGVKIT FFHGRGGTVG RGGGPTYEAI
     TSQPLRSIND RIRLTEQGEV IGNKYGNKDA AYYNLEMLVS AAINRMVTHK KSDAHTSNKY
     ERIMDQVVER SYQIYRDLVF GDERFYDYFF ESSPIKAISS FNIGSRPAAR KTITEIGGLR
     AIPWVFSWSQ SRVMFPGWYG VGSSFKEFID QDPENNLAFL QLMYKRWPFF KSLLSNVDMV
     LSKSNMNIAF EYAQLCEDQN VRDIFNIILD EWQLTKNVIL EIEGHDELLA ENTYLRDSLD
     YRMPYFNVLN YIQLELIKRQ RNGQLTPDQE KLIHITINGI ATGLRNSG