CAPP_STRTD
ID CAPP_STRTD Reviewed; 940 AA.
AC Q03LA9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=STER_0760;
OS Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=322159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-491 / LMD-9;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00595}.
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DR EMBL; CP000419; ABJ66013.1; -; Genomic_DNA.
DR RefSeq; WP_011680994.1; NC_008532.1.
DR AlphaFoldDB; Q03LA9; -.
DR SMR; Q03LA9; -.
DR KEGG; ste:STER_0760; -.
DR HOGENOM; CLU_006557_2_0_9; -.
DR OMA; PWVFGWT; -.
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 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; PTHR30523; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation; Lyase; Magnesium.
FT CHAIN 1..940
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_1000025598"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 603
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
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