ID   I1ZMY9_STRPA            Unreviewed;       941 AA.
AC   I1ZMY9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=Spaf_1440 {ECO:0000313|EMBL:AFJ26413.1};
OS   Streptococcus parasanguinis FW213.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1114965 {ECO:0000313|EMBL:AFJ26413.1, ECO:0000313|Proteomes:UP000002865};
RN   [1] {ECO:0000313|EMBL:AFJ26413.1, ECO:0000313|Proteomes:UP000002865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FW213 {ECO:0000313|EMBL:AFJ26413.1,
RC   ECO:0000313|Proteomes:UP000002865};
RX   PubMed=22529932; DOI=10.1371/journal.pone.0034769;
RA   Geng J., Chiu C.H., Tang P., Chen Y., Shieh H.R., Hu S., Chen Y.Y.;
RT   "Complete Genome and Transcriptomes of Streptococcus parasanguinis FW213:
RT   Phylogenic Relations and Potential Virulence Mechanisms.";
RL   PLoS ONE 7:E34769-E34769(2012).
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; CP003122; AFJ26413.1; -; Genomic_DNA.
DR   RefSeq; WP_014713627.1; NC_017905.1.
DR   AlphaFoldDB; I1ZMY9; -.
DR   STRING; 1114965.Spaf_1440; -.
DR   PaxDb; 1114965-Spaf_1440; -.
DR   KEGG; scf:Spaf_1440; -.
DR   PATRIC; fig|1114965.3.peg.1385; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000002865; 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:AFJ26413.1}.
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;  107911 MW;  A7DECA0778EBAC29 CRC64;
     MVLQKLENFR NKDIVKEEAE ILTDLLDDIT KNLVCPETFE KISQLKDLSK TKNYRDLNQL
     VEQLSNEEMT VISRYFAILP LLINISEDVD LAYEINHLNN VDGDYLGKLS STIKEVAKNE
     DAQEILENLN IVPVLTAHPT QVQRKTMLDL TNHIHALLRQ HRDVKAGLIN ENKWYNNLRC
     NIEIMMQTDM IRDKKLKVTN EITNVMEYYN SSFLQAVPNL VLEYKRLAKE HGLELEQPHP
     ITMGMWIGGD RDGNPFVTAD TLKRSATIQS EVILNYYIEK ISKLYRHFSL STSLSNTSEA
     VAEMAALSSD TSVFREKEPY RRAFHYIQSK LIQTLVNLKE WTMVGETRED RYAVERLLGA
     SNHQQGPVSD YIGNRISGAL KEISAKESPA YASAQEFKED LEKIKDSLLE NKSEYLISGE
     FAELLEAIDV FGFYLASIDM RQDSSVHEAC VAELLKSAGI NDHYSDLSED EKCQILLKEL
     LEDPRILSAT HADKSELLEK ELAIFQTARE LKDRLGEEVI RQNIISHATS VSDMLELAVM
     LKEVGLIDTE KARVQIVPLF ETIEDLDHSE ETMRSYLSLP IAKRWIASKN NYQEIMLGYS
     DSNKDGGYLS SCWTLFKAQQ QLTAIGDEFG VKITFFHGRG GTVGRGGGPT YEAITSQPLK
     SINDRIRLTE QGEVIGNKYG NKDAAYYNLE MLVSATINRM IAEQKSPFSM FDRFGEVMDK
     VVNRSYDIYR DLVFGNEHFY DYFFESSPIK AISSFNIGSR PAARKTITEI GGLRAIPWVF
     SWSQSRVMFP GWYGVGSSFK EFIDEDPENI ETLRYMYKNW PFFQSLLSNV DMVLSKANMD
     IAFEYAQLCE EEEVRNIYQI ILHEWQLTKD IILMIEEQEE LLAENSYLKE SLDYRMPYFN
     VLNYIQLELI RRQRTGQLPA DQDKLIHITI NGVATGLRNS G
//