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Database: UniProt/SWISS-PROT
Entry: CAPP_STRA5
LinkDB: CAPP_STRA5
Original site: CAPP_STRA5 
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   22-NOV-2017, entry version 80.
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; Firmicutes; 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.,
RA   Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S.,
RA   Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M.,
RA   Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D.,
RA   Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G.,
RA   Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an
RT   emerging 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
CC       source for the tricarboxylic acid cycle. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000255|HAMAP-
CC       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.
CC       {ECO:0000255|HAMAP-Rule:MF_00595}.
DR   EMBL; AE009948; AAM99646.1; -; Genomic_DNA.
DR   RefSeq; NP_687774.1; NC_004116.1.
DR   RefSeq; WP_000019267.1; NC_004116.1.
DR   ProteinModelPortal; Q8E0H2; -.
DR   SMR; Q8E0H2; -.
DR   EnsemblBacteria; AAM99646; AAM99646; SAG0759.
DR   GeneID; 1013563; -.
DR   KEGG; sag:SAG0759; -.
DR   PATRIC; fig|208435.3.peg.765; -.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000000821; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
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; 2.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation; Complete proteome; Lyase; Magnesium;
KW   Reference proteome.
FT   CHAIN         1    931       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000166626.
FT   ACT_SITE    138    138       {ECO:0000255|HAMAP-Rule:MF_00595}.
FT   ACT_SITE    594    594       {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
//
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