ID   CAPP_STRT2              Reviewed;         940 AA.
AC   Q5M4Z3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=stu0718;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000023; AAV60411.1; -; Genomic_DNA.
DR   RefSeq; WP_011225765.1; NC_006448.1.
DR   AlphaFoldDB; Q5M4Z3; -.
DR   SMR; Q5M4Z3; -.
DR   STRING; 264199.stu0718; -.
DR   GeneID; 66898618; -.
DR   KEGG; stl:stu0718; -.
DR   PATRIC; fig|264199.4.peg.726; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000001170; 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..940
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166637"
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;  107129 MW;  C4EA21A15C77E442 CRC64;
     MAFNKLESSN NQEIISEEVG ILKELLDDAT RGMAGEQGLT 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 GNFSKERAAK 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 LTNIGEERGI KITFFHGRGG TVGRGGGPSY DAITSQPFGT
     IKDRIRLTEQ GEVIGNKYGN KDAAYYNLEM LVSATLDRMV TRQITDPDEL VDFREIMDSI
     VQDSNRIYRD LVFGNEHFYD YFFEASPIKE VSSLNIGSRP AARKTITDIS GLRAIPWVFS
     WSQNRIMLPG WYGVGSAFNH YIEAEEGNLE KLQHMFETWP FFRSLLSNVD MVLSKSDMNI
     AFHYAQLAES EEVRSVFNII LDEWQLTKNV ILAIEKHDDF LEESPSLKAS LGFRLPYFNV
     LNYIQIELIK RLRNNNLTDD EISLIHITIN GIATGLRNSG
//