ID   C1CE55_STRZJ            Unreviewed;       898 AA.
AC   C1CE55;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
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:ACO18080.1};
GN   OrderedLocusNames=SPJ_1006 {ECO:0000313|EMBL:ACO18080.1};
OS   Streptococcus pneumoniae (strain JJA).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=488222 {ECO:0000313|EMBL:ACO18080.1, ECO:0000313|Proteomes:UP000002206};
RN   [1] {ECO:0000313|Proteomes:UP000002206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JJA {ECO:0000313|Proteomes:UP000002206};
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000919; ACO18080.1; -; Genomic_DNA.
DR   RefSeq; WP_000058193.1; NC_012466.1.
DR   AlphaFoldDB; C1CE55; -.
DR   KEGG; sjj:SPJ_1006; -.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   Proteomes; UP000002206; 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:ACO18080.1}.
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;  103286 MW;  B99E87C049DD4F0D CRC64;
     MSLQKLENYS NKSVVQEEVL ILTELLEDIT KNMLAPETFE KIIQLKELST QEDYQGLNRL
     VTSLSNDEMV YISRYFSILP LLINISEDVD LAYEINHQNN IDQDYLGKLS TTIKLVAEKE
     NAVEILEHLN VVPVLTAHPT QVQRKSMLDL TNHIHSLLRK YRDVKLGLIN KDKWYNDLRR
     YIEIIMQTDM IREKKLKVTN EITNAMEYYN SSFLKAVPHL TTEYKRLAQA HGLNLKQAKP
     ITMGMWIGGD RDGNPFVTAE TLKQSALTQC EVIMNYYDKK IYQLYREFSL STSIVNVSKQ
     VREMARQSKD NSIYREKELY RRALFDIQSK IQATKTYLIE DEEVGTRYET ANDFYKDLIA
     IRDSLLENKG ESLISGDFVE LLQAVEIFGF YLASIDMRQD SSVYEACVAE LLKSAGIHSR
     YSELSEEEKC DLLLKELEED PRILSATHAE KSELLAKELA IFKTARVLKD KLGDDVIRQT
     IISHATSLSD MLELAILLKE VGLVDTERAR VQIVPLFETI EDLDHSEETM RKYLSLSLAK
     KWIDSRNNYQ EIMLGYSDSN KDGGYLSSCW TLYKAQQQLT AIGDEFGVKV TFFHGRGGTV
     GRGGGPTYEA ITSQPLKSIK DRIRLTEQGE VIGNKYGNKD AAYYNLEMLV SAAINRMITQ
     KKSDTNTPNR YEAIMDQVVD RSYDIYRDLV FGNEHFYDYF FESSPIKAIS SFNIGSRPAA
     RKTITEIGGL RAIPWVFSWS QSRVMFPGWY GVGSSFKEFI NKNPENIAIL RDMYQNWPFF
     QSLLSNVDMV LSKSNMNIAF EYAKLCEDEQ VKAIYETILN EWQVTKNVIL AIEGHDELLA
     DNPYLKASLD YRMPYFNILN YIQLELIKRQ RRGELSSDQE RLIHITINGI ATGLRNSG
//