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Database: UniProt/SWISS-PROT
Entry: CAPP_STRA1
LinkDB: CAPP_STRA1
Original site: CAPP_STRA1 
ID   CAPP_STRA1              Reviewed;         931 AA.
AC   Q3K1U6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   22-NOV-2017, entry version 74.
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};
GN   OrderedLocusNames=SAK_0885;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S.,
RA   DeBoy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I.,
RA   Peterson J.D., Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A.,
RA   Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N.,
RA   Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J.,
RA   Smith S., Utterback T.R., White O., Rubens C.E., Grandi G.,
RA   Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R.,
RA   Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
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; CP000114; ABA45567.1; -; Genomic_DNA.
DR   RefSeq; WP_000019270.1; NC_007432.1.
DR   SMR; Q3K1U6; -.
DR   EnsemblBacteria; ABA45567; ABA45567; SAK_0885.
DR   KEGG; sak:SAK_0885; -.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
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; Lyase; Magnesium.
FT   CHAIN         1    931       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_1000025592.
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;  105936 MW;  93AEEB65705C8480 CRC64;
     MSHPKLESSS NKEIITEEVG LLKQLLDEAT QKLIGSESFD KIEKIVSLSS 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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