ID C1C765_STRP7 Unreviewed; 898 AA.
AC C1C765;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 81.
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:ACO16784.1};
GN OrderedLocusNames=SP70585_1142 {ECO:0000313|EMBL:ACO16784.1};
OS Streptococcus pneumoniae (strain 70585).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488221 {ECO:0000313|EMBL:ACO16784.1, ECO:0000313|Proteomes:UP000002211};
RN [1] {ECO:0000313|Proteomes:UP000002211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70585 {ECO:0000313|Proteomes:UP000002211};
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,
CC ECO:0000256|HAMAP-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; CP000918; ACO16784.1; -; Genomic_DNA.
DR RefSeq; WP_000058195.1; NC_012468.1.
DR AlphaFoldDB; C1C765; -.
DR KEGG; snm:SP70585_1142; -.
DR HOGENOM; CLU_006557_2_0_9; -.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000002211; 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:ACO16784.1}.
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; 103272 MW; CCFF7B7528242B56 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 RSYDVYRDLV FGNEHFYDYF FESSPIKAIS SFNIGSRPAA
RKTITEIGGL RAIPWVFSWS QSRVMFPGWY GVGSSFKEFI NKNPENIAIL RDMYQNWPFF
QSLLSNVDMV LSKSNMNIAF EYAKLCEDEQ VKAIYETILN EWQVTKNVIL AIEGHDELLA
DNPYLKASLD YRMPYFNILN YIQLELIKRQ RRGELSSDQE RLIHITINGI ATGLRNSG
//