CAPP_STRPQ
ID CAPP_STRPQ Reviewed; 920 AA.
AC P0DC99; Q8K873;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 41.
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=SPs1425;
OS Streptococcus pyogenes serotype M3 (strain SSI-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=193567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSI-1;
RX PubMed=12799345; DOI=10.1101/gr.1096703;
RA Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA Hattori M., Hamada S.;
RT "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT scale genomic rearrangement in invasive strains and new insights into phage
RT evolution.";
RL Genome Res. 13:1042-1055(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC64520.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000034; BAC64520.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P0DC99; -.
DR SMR; P0DC99; -.
DR KEGG; sps:SPs1425; -.
DR HOGENOM; CLU_006557_2_0_9; -.
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..920
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000411437"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 583
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 920 AA; 104699 MW; A7837E73861919F7 CRC64;
MPLKKLESSN NQTIIAEEVA LLKEMLENIT RRMIGDDAFT VIESIMVLSE KQDYIELEKV
VANISNQEME VISRYFSILP LLINISEDVD LAYEINHQNN TDTDYLGKLA LTIKDLAGKD
NGKDILEQVN VVPVLTAHPT QVQRKTILEL TTHIHKLLRK YRDAKAGVIN LEKWRQELYR
YIEMIMQTDI IREKKLQVKN EIKNVMQYYD GSLIQAVTKL TTEYKNLAQK HGLELDNPKP
ITMGMWIGGD RDGNPFVTAE TLCLSATVQS EVILNYYIDK LAALYRTFSL SSTLVQPNSE
VERLASLSQD QSIYRGNEPY RRAFHYIQSR LKQTQIQLTN QPAARMSSSV GLNTSAWSSP
ASLENPILAY DSPVDFKADL KAIEQSLLDN GNSALIEGDL REVMQAVDIF GFFLASIDMR
QDSSVQEACV AELLKGANIV DDYSSLSETE KCDVLLQQLM EEPRTLSSAA VAKSDLLEKE
LAIYTTAREL KDKLGEEVIK QHIISHTESV SDMFELAIML KEVGLVDQQR ARVQIVPLFE
TIEDLDNARD IMAAYLSHDI VKSWIATNRN YQEIMLGYSD SNKDGGYLAS GWTLYKAQNE
LTAIGEEHGV KITFFHGRGG TVGRGGGPSY DAITSQPFGS IKDRIRLTEQ GEIIENKYGN
KDVAYYHLEM LISASINRMV TQMITDPNEI DSFREIMDSI VADSNTIYRK LVFDNPHFYD
YFFEASPIKE VSSLNIGSRP AARKTITEIT GLRAIPWVFS WSQNRIMFPG WYGVGSAFKR
YIDRAQGNLE RLQHMYQTWP FFHSLLSNVD MVLSKSNMNI AFQYAQLAES QDVRDVFYEI
LDEWQLTKNV ILAIQDHDDL LEDNPSLKHS LKSRLPYFNV LNYIQIELIK RWRNNQLDEN
DEKLIHTTIN GIATGLRNSG