ID   F5X2D8_STRPX            Unreviewed;       941 AA.
AC   F5X2D8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:BAK30447.1};
GN   OrderedLocusNames=SGPB_1409 {ECO:0000313|EMBL:BAK30447.1};
OS   Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK30447.1, ECO:0000313|Proteomes:UP000007946};
RN   [1] {ECO:0000313|EMBL:BAK30447.1, ECO:0000313|Proteomes:UP000007946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC   {ECO:0000313|Proteomes:UP000007946};
RX   PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA   Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA   Chang C.-H., Hsu M.-T.;
RT   "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT   gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL   PLoS ONE 6:E20519-E20519(2011).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|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:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; AP012054; BAK30447.1; -; Genomic_DNA.
DR   RefSeq; WP_013852088.1; NC_015600.1.
DR   AlphaFoldDB; F5X2D8; -.
DR   STRING; 981540.SGPB_1409; -.
DR   GeneID; 76468854; -.
DR   KEGG; stb:SGPB_1409; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000007946; 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 {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:BAK30447.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007946}.
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        604
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   941 AA;  107545 MW;  E37C4E2CF4594FB8 CRC64;
     MTIKKLENNS TQSIITEEVK VLKDLLDEAT HQMVGDEVFA KIQNIVELSA SDEYVKLEKL
     VAQLTNDEMV VVSRYFSILP LLINISEDVD FAYEINYQNN TNQDYLGKLS LTVDMVSESE
     NSKEILENVN VVPVLTAHPT QVQRKTVLEL TNHIHDLLRK YRDVRAGVVN RDKWYTDLRR
     YIEIIMQTDI IREKKLKVKN EITNVMEYYN TSLIQAITKL TSEYKRLAAE KGIDLEDPKP
     ITMGMWIGGD RDGNPYVTAE TLRLSATVQS EVIINYYIEK LTGLYRTFSL STTLTNISPE
     VEKLAELSSD KSIYRENEPY RKAFNYIQSK LIQTLIELKA SPAISQRVLE SSNSISSDVY
     TSTNNASVIT KYLQTKFSKV SSELQEEIPS YKTAKEFKDD LLIIKQSLLD NGDDALLIGD
     FSELLQAVEV FGFYLAMIDM RQDSSVNEAC VAELLKSANI VEDYSALSEE EKVKVLLKEL
     QEDPRTLSST NAEKSEQLQK ELAIFQTARY LKDKLGDEVI KQHIISHTES VSDMFELAIM
     LKEVGLLDNQ KARVQIVPLF ETIEDLENSR AIMEEYLDYD IVRRWVSANK GYQEIMLGYS
     DSNKDGGYLS SVWTLYKAQN ELTRIGSERG IKVTFIHGRG GTVGRGGGPS YEAITSQPFG
     SIKDRIRLTE QGEIIENKYG NKDVAYYNLE MLVSATIDRI VTRMITNPDE IDDFRATMDG
     IVTYSNSVYR DLVFGNPHFY DYFFEATPIK EVSSLNIGSR PAARKTITEI SGLRAIPWVF
     SWSQSRIMFP GWYGVGSAFK NFIDAEEGNL AKLQHMYEKW PFFHSLLSNV DMVLSKSNMN
     IAFQYAQLAE SEEVRDVFNT ILDEWQLTKN VILAIEKHED LLEENPSLQA SLDYRLPYFN
     VLNYIQIELI KRLRHEELDE DYEKLIHTTI NGIATGLRNS G
//