ID   G7SFD4_STRSU            Unreviewed;       898 AA.
AC   G7SFD4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
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   ORFNames=SSUD12_0519 {ECO:0000313|EMBL:AER18842.1};
OS   Streptococcus suis D12.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1004952 {ECO:0000313|EMBL:AER18842.1, ECO:0000313|Proteomes:UP000008845};
RN   [1] {ECO:0000313|EMBL:AER18842.1, ECO:0000313|Proteomes:UP000008845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D12 {ECO:0000313|EMBL:AER18842.1};
RX   PubMed=22026465; DOI=10.1186/1471-2164-12-523;
RA   Zhang A., Yang M., Hu P., Wu J., Chen B., Hua Y., Yu J., Chen H., Xiao J.,
RA   Jin M.;
RT   "Comparative Genomic Analysis of Streptococcus suis reveals significant
RT   genomic diversity among different serotypes.";
RL   BMC Genomics 12:523-523(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002644; AER18842.1; -; Genomic_DNA.
DR   RefSeq; WP_014637614.1; NC_017621.1.
DR   AlphaFoldDB; G7SFD4; -.
DR   KEGG; ssk:SSUD12_0519; -.
DR   PATRIC; fig|1004952.3.peg.503; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000008845; 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:AER18842.1}.
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        561
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   898 AA;  102862 MW;  9ABD6CC668726CF3 CRC64;
     MAIQKLENYN NKEAIREEVT ILTSILEEVA AQMMPAETFA KIVELSQLSR QDDYQALIAI
     ISQLNNDELA VISRYFAVLP LLINISEDVD LAYEINHQNN IDQDYLGKIS TTIDMVSKQE
     NAAEILEKLN VVPVLTAHPT QVQRQSMLDL TKHIHELLRR YRDVKLGLLN KNKWEDELRC
     YIEIIMQTDM IREKKLKVTN EITNVMEYYN SSFIKAVTKL QREYKRLAAE KGIVLNNPRP
     ITMGMWIGGD RDGNPFVTAE TLKLSALTQC EVIMNYYDEQ LYKLYRNFSL STSIVNVSTA
     VKMLADLSED SSVYRENEPY RRAFHYIQMK LANTRDYLVH NKPSDVRYSN VAEFKADLLA
     IKQSLIENKS MALLKGDFTE LLEAVEAFGF YLASIDMRQD SSIHEASVAE LLASARIVED
     YSSLSEEAKC HVLLKQLETD PRILSATHIP KSEQLEKELA IFAAARELKD KLGEEIIKQH
     IISHSESVSD LLELAVLLKE VGLVDVDKAR VQIVPLFETI EDLDNAPDTM RQYLQLDLAK
     RWIAGNKYYQ EIMLGYSDSN KDGGYLSSGW TLYKAQNELT QIGQDYGVNI TFFHGRGGTV
     GRGGGPSYDA ITSQPFGSIK DRLRLTEQGE VIGNKYGNKD AAYYNLEMLV SATLDRMVTQ
     MITDPNEIDG YRETMDEIVS DSYRIYRDLV FNNPHFYDYF FAASPIREVS SLNIGSRPAA
     RKTITEIGGL RAIPWVFSWS QNRVMLPGWY GVGSSFKRFI DKHPDNLSKL QKMYESWPFF
     RSLLSNVDMV LSKSNMNIAF EYAKMCESEE VRNIFHVILD EWQLTKEIIL SIEQNDELLA
     ELPFLKASLD YRMPYFNVLN YIQIELIHRL RRGELSKEQE NLIHITINGV ATGLRNSG
//