ID   CAPP_STRA5              Reviewed;         931 AA.
AC   Q8E0H2;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=SAG0759;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(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; Evidence={ECO:0000255|HAMAP-
CC         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; AE009948; AAM99646.1; -; Genomic_DNA.
DR   RefSeq; NP_687774.1; NC_004116.1.
DR   RefSeq; WP_000019267.1; NC_004116.1.
DR   AlphaFoldDB; Q8E0H2; -.
DR   SMR; Q8E0H2; -.
DR   STRING; 208435.SAG0759; -.
DR   KEGG; sag:SAG0759; -.
DR   PATRIC; fig|208435.3.peg.765; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000821; 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..931
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166626"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        594
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   931 AA;  105962 MW;  F5338365FADF9B2C CRC64;
     MSHPKLESSS NKEIITEEVG LLKQLLDEAT QKLIGSESFD KIEKIVSLSL TDDYTGLKET
     ISALSNEEMV IVSRYFSILP LLINISEDVD LAYEINYKNN LNQDYLGKLS TTIDVVAGHE
     NAKDILEHVN VVPVLTAHPT QVQRKTVLEL TSKIHDLLRK YRDVKAGIVN QEKWYADLRR
     YIGIIMQTDT IREKKLKVKN EITNVMEYYN RSLIKAVTKL TAEYKALAAK KGIHLENPKP
     LTMGMWIGGD RDGNPFVTAE TLRLSAMVQS EVIINHYIEQ LNELYRNMSL SINLTEVSPE
     LVTLANQSQD NSVYRENEPY RKAFNFIQDK LVQTLLNLKV GSSPKEKFVS RQESSDIVGR
     YIKSHIAQVA SDIQTEELPA YATAEEFKQD LLLVKQSLVQ YGQDSLVDGE LACLIQAVDI
     FGFYLATIDM RQDSSINEAC VAELLKSANI VDDYSSLSEE EKCQLLLKEL TEDPRTLSST
     HAPKSELLQK ELAIFQTARE LKDQLGEDII NQHIISHTES VSDMFELAIM LKEVGLIDAN
     QARIQIVPLF ETIEDLDNSR DIMTQYLHYE LVKKWIATNN NYQEIMLGYS DSNKDGGYLS
     SGWTLYKAQN ELTKIGEENG IKITFFHGRG GTVGRGGGPS YEAITSQPFG SIKDRIRLTE
     QGEIIENKYG NQDAAYYNLE MLISASIDRM VTRMITNPNE IDNFRETMDG IVSESNAVYR
     NLVFDNPYFY DYFFEASPIK EVSSLNIGSR PAARKTITEI SGLRAIPWVF SWSQNRIMFP
     GWYGVGSAFK HFIEQDEANL AKLQTMYQKW PFFNSLLSNV DMVLSKSNMN IALQYAQLAG
     SKEVRDVFNI ILNEWQLTKD MILAIEQHDN LLEENPMLHA SLDYRLPYFN VLNYVQIELI
     KRLRSNQLDE DYEKLIHITI NGIATGLRNS G
//