ID   D5AGL8_STRGZ            Unreviewed;       898 AA.
AC   D5AGL8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
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   OrderedLocusNames=SSGZ1_0518 {ECO:0000313|EMBL:ADE30983.1};
OS   Streptococcus suis (strain GZ1).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=423211 {ECO:0000313|EMBL:ADE30983.1, ECO:0000313|Proteomes:UP000002359};
RN   [1] {ECO:0000313|EMBL:ADE30983.1, ECO:0000313|Proteomes:UP000002359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GZ1 {ECO:0000313|EMBL:ADE30983.1,
RC   ECO:0000313|Proteomes:UP000002359};
RX   PubMed=19016627; DOI=10.1086/594370;
RA   Ye C., Zheng H., Zhang J., Jing H., Wang L., Xiong Y., Wang W., Zhou Z.,
RA   Sun Q., Luo X., Du H., Gottschalk M., Xu J.;
RT   "Clinical, experimental, and genomic differences between intermediately
RT   pathogenic, highly pathogenic, and epidemic Streptococcus suis.";
RL   J. Infect. Dis. 199:97-107(2009).
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; CP000837; ADE30983.1; -; Genomic_DNA.
DR   RefSeq; WP_011922076.1; NC_017617.1.
DR   AlphaFoldDB; D5AGL8; -.
DR   SMR; D5AGL8; -.
DR   KEGG; ssw:SSGZ1_0518; -.
DR   PATRIC; fig|423211.3.peg.508; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000002359; 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:ADE30983.1}.
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;  102866 MW;  678102D294644EFD 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
     IKQSLVENKS MALLKGDFTE LLEAVEAFGF YLASIDMRQD SSIHEASVAE LLASARIVED
     YSSLSEEAKC HVLLKQLETD PRILSATHMP 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
//