ID F8LWI1_STRTR Unreviewed; 940 AA.
AC F8LWI1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
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:CCC19618.1};
GN ORFNames=STH8232_0911 {ECO:0000313|EMBL:CCC19618.1};
OS Streptococcus thermophilus JIM 8232.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1051074 {ECO:0000313|EMBL:CCC19618.1, ECO:0000313|Proteomes:UP000000300};
RN [1] {ECO:0000313|EMBL:CCC19618.1, ECO:0000313|Proteomes:UP000000300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JIM 8232 {ECO:0000313|EMBL:CCC19618.1,
RC ECO:0000313|Proteomes:UP000000300};
RA Renault P., Loux V.;
RT "Complete genome sequence of Streptococcus thermophilus strain JIM8232.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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; FR875178; CCC19618.1; -; Genomic_DNA.
DR RefSeq; WP_011680994.1; NC_017581.1.
DR AlphaFoldDB; F8LWI1; -.
DR SMR; F8LWI1; -.
DR KEGG; stu:STH8232_0911; -.
DR PATRIC; fig|1051074.3.peg.775; -.
DR HOGENOM; CLU_006557_2_0_9; -.
DR Proteomes; UP000000300; 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:CCC19618.1}.
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 603
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 940 AA; 107012 MW; 369DE223D6E0E59A CRC64;
MAFNKLESSN NQEIISEEVG ILKELLDDAT RGIAGEQGLT TIQHLVELYD EGDYEALTQA
ISEMTNDDMV VASRYFSLLP LLINISEDVD LAYEVNRKNN IDESYLGKLS ETFDVVAESD
NARDILENVN VVPVLTAHPT QVQRKTMLEL TNHIHELLRK HRDVKDGLIN KDKWYADLRR
YVEIMMKTDI IREKKLKVKN EITNVMEYYN SSLIKAITKL SHEFKRLAVE KGIELDNPTP
ITMGMWIGGD RDGNPFVTAE TLKLSATLQS EVILNYYIEK VDNLYRSFSL SSRLTEVSET
VAEMAKLSPD TSVYRENEPY RRAFSYIQSK LIQTLLFFKA GNFSNERAAK RLSENVRLGS
VSTGEVVADF VHDRLSQSLQ AVSQQTTEFY ETAEAFHDDL LAIKNSLLEN DDSVLISGDF
EELLQAVEVF GFYLATIDMR QDSSVHEACV AELLKSANIV DNYSELTEVE KVAVLLKELQ
EDPRTLSSTN VSKSETLEKE LAIFRTARLL KDYLGEEVIK QHIISHTESV SDMFELAILL
KEVGLVDTER ARVQIVPLFE TIEDLENSNE IMKQYLGYDI VKRWIKNSNN YQEIMLGYSD
SNKDGGYLSS GWTLYKAQNE LTKIGEERGI KITFFHGRGG TVGRGGGPSY DAITSQPFGT
IKDRIRLTEQ GEVIGNKYGN KDAAYYNLEM LVSATLDRMV TRQITDPDEL VDFREIMDSI
VQDSNGIYRD LVFGNEHFYD YFFEASPIKE VSSLNIGSRP AARKTITDIS GLRAIPWVFS
WSQNRIMLPG WYGVGSAFNH YIEAEEGNLE KLQHMFETWP FFRSLLSNVD MVLSKSDMNI
AFHYAQLAES EEVRSVFNII LDEWQLTKNV ILAIEKHDDF LEESPSLKAS LGFRLPYFNV
LNYIQIELIK RLRNNNLTDD EISLIHITIN GIATGLRNSG
//