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   27-MAR-2024, entry version 86.
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; Bacillota; 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., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., 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 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; CP000419; ABJ66013.1; -; Genomic_DNA.
DR   RefSeq; WP_011680994.1; NC_008532.1.
DR   AlphaFoldDB; Q03LA9; -.
DR   SMR; Q03LA9; -.
DR   KEGG; ste:STER_0760; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
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.
FT   CHAIN           1..940
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025598"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        603
FT                   /evidence="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
//