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Database: UniProt/SWISS-PROT
Entry: CAPP_STRTD
LinkDB: CAPP_STRTD
Original site: CAPP_STRTD 
ID   CAPP_STRTD              Reviewed;         940 AA.
AC   Q03LA9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   05-DEC-2018, entry version 73.
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=STER_0760;
OS   Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=322159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-491 / LMD-9;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702;
CC         EC=4.1.1.31; 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00595}.
DR   EMBL; CP000419; ABJ66013.1; -; Genomic_DNA.
DR   RefSeq; WP_011680994.1; NC_008532.1.
DR   ProteinModelPortal; Q03LA9; -.
DR   SMR; Q03LA9; -.
DR   EnsemblBacteria; ABJ66013; ABJ66013; STER_0760.
DR   GeneID; 31937564; -.
DR   KEGG; ste:STER_0760; -.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
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.
FT   CHAIN         1    940       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_1000025598.
FT   ACT_SITE    138    138       {ECO:0000255|HAMAP-Rule:MF_00595}.
FT   ACT_SITE    603    603       {ECO:0000255|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   940 AA;  107012 MW;  369DE223D6E0E59A CRC64;
     MAFNKLESSN NQEIISEEVG ILKELLDDAT RGIAGEQGLT TIQHLVELYD EGDYEALTQA
     ISEMTNDDMV VASRYFSLLP LLINISEDVD LAYEVNRKNN IDESYLGKLS ETFDVVAESD
     NARDILENVN VVPVLTAHPT QVQRKTMLEL TNHIHELLRK HRDVKDGLIN KDKWYADLRR
     YVEIMMKTDI IREKKLKVKN EITNVMEYYN SSLIKAITKL SHEFKRLAVE KGIELDNPTP
     ITMGMWIGGD RDGNPFVTAE TLKLSATLQS EVILNYYIEK VDNLYRSFSL SSRLTEVSET
     VAEMAKLSPD TSVYRENEPY RRAFSYIQSK LIQTLLFFKA GNFSNERAAK RLSENVRLGS
     VSTGEVVADF VHDRLSQSLQ AVSQQTTEFY ETAEAFHDDL LAIKNSLLEN DDSVLISGDF
     EELLQAVEVF GFYLATIDMR QDSSVHEACV AELLKSANIV DNYSELTEVE KVAVLLKELQ
     EDPRTLSSTN VSKSETLEKE LAIFRTARLL KDYLGEEVIK QHIISHTESV SDMFELAILL
     KEVGLVDTER ARVQIVPLFE TIEDLENSNE IMKQYLGYDI VKRWIKNSNN YQEIMLGYSD
     SNKDGGYLSS GWTLYKAQNE LTKIGEERGI KITFFHGRGG TVGRGGGPSY DAITSQPFGT
     IKDRIRLTEQ GEVIGNKYGN KDAAYYNLEM LVSATLDRMV TRQITDPDEL VDFREIMDSI
     VQDSNGIYRD LVFGNEHFYD YFFEASPIKE VSSLNIGSRP AARKTITDIS GLRAIPWVFS
     WSQNRIMLPG WYGVGSAFNH YIEAEEGNLE KLQHMFETWP FFRSLLSNVD MVLSKSDMNI
     AFHYAQLAES EEVRSVFNII LDEWQLTKNV ILAIEKHDDF LEESPSLKAS LGFRLPYFNV
     LNYIQIELIK RLRNNNLTDD EISLIHITIN GIATGLRNSG
//
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