ID   F2QDV4_STROU            Unreviewed;       898 AA.
AC   F2QDV4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
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:CBZ00823.1};
GN   OrderedLocusNames=SOR_1165 {ECO:0000313|EMBL:CBZ00823.1};
OS   Streptococcus oralis (strain Uo5).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=927666 {ECO:0000313|EMBL:CBZ00823.1, ECO:0000313|Proteomes:UP000008131};
RN   [1] {ECO:0000313|EMBL:CBZ00823.1, ECO:0000313|Proteomes:UP000008131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uo5 {ECO:0000313|EMBL:CBZ00823.1,
RC   ECO:0000313|Proteomes:UP000008131};
RX   PubMed=21460080; DOI=10.1128/JB.00321-11;
RA   Reichmann P., Nuhn M., Denapaite D., Bruckner R., Henrich B., Maurer P.,
RA   Rieger M., Klages S., Reinhard R., Hakenbeck R.;
RT   "Genome of Streptococcus oralis strain Uo5.";
RL   J. Bacteriol. 193:2888-2889(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; FR720602; CBZ00823.1; -; Genomic_DNA.
DR   RefSeq; WP_000058161.1; NC_015291.1.
DR   AlphaFoldDB; F2QDV4; -.
DR   KEGG; sor:SOR_1165; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000008131; 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:CBZ00823.1}.
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;  103342 MW;  CE281089C983BD43 CRC64;
     MSLQKLENYS NKAVVQEEVL ILTELLEDIT KNMLAPETFE KIIQLKELST SEDYQGLNDL
     VTSLSNEEMI YISRYFSILP LLINISEDVD LAYEINHQNN VDQDYLGKLS TTIKMVAEKE
     NAAEILEKLN VVPVLTAHPT QVQRKSMLDL TNHIHTLLRK YRDVKLGLIN KEKWHTDLRR
     YIEIIMQTDM IREKKLKVTN EITNVMEYYQ SSFLNAVPRL TAEYKKMAKE QGIDLQHPKP
     ITMGMWIGGD RDGNPFVTAE TLNKSALTQC EVIMNYYDEK IYNLYREFSL STSIVNVSDK
     VREMALKSQD NSIYREKELY RRALFDIQAK MQATKAYLIE DKELQPRYAT ADEFYQDLLA
     IRDSLLENKG EYLISGEFVE LMQAVEIFGF YLASIDMRQD SSVHEACVAE LLASAGINDH
     YSDLSEDEKC TLLLKELEED PRILSATHAQ KSELLEKELS IFKAARKLKD KLGENVIRQT
     IISHATSVSD MLELAIMLKE VGLVDAQKAR VQIVPLFETI EDLDHSEETM RRYFSLPLAK
     KWIASKDNYQ EIMLGYSDSN KDGGYLSSCW TLYKAQQQLT AIGDEFGVKV TFFHGRGGTV
     GRGGGPTYEA ITSQPLKSIK DRIRLTEQGE VIGNKYGNKD AAYYNLEMLV SAAINRMITK
     KKSDTNTSNR YEAIMDQVVD RSYDIYRDLV FGNEHFYDYF FESSPIKAIS SFNIGSRPAA
     RKTITEIGGL RAIPWVFSWS QSRVMFPGWY GVGSSFKEFI DQDPKNIEFL RDMYQNWPFF
     QSLLSNVDMV LSKSNMNIAF EYAKLCEDEE VQAIYYTILD EWQLTKDVIL AIEGYDELLA
     ENSYLKDSLN YRMPYFNILN YIQLELIKRQ RRGELSADEE KLIHTTINGI ATGLRNSG
//