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Database: UniProt/SWISS-PROT
Entry: CAPP_STRP1
LinkDB: CAPP_STRP1
Original site: CAPP_STRP1 
ID   CAPP_STRP1              Reviewed;         920 AA.
AC   Q9A0U7; Q48ZU5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 2.
DT   20-JUN-2018, entry version 101.
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};
GN   OrderedLocusNames=SPy_0608, M5005_Spy0505;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J.,
RA   Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   SEQUENCE REVISION TO 345.
RA   Beres S.B., Musser J.M.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J.,
RA   Hoe N.P., Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of
RT   serotype M1 group A Streptococcus involved multiple horizontal gene
RT   transfer events.";
RL   J. Infect. Dis. 192:771-782(2005).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000255|HAMAP-
CC       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.
CC       {ECO:0000255|HAMAP-Rule:MF_00595}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ51123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE004092; AAK33584.2; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51123.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_268863.2; NC_002737.2.
DR   SMR; Q9A0U7; -.
DR   STRING; 160490.SPy_0608; -.
DR   PaxDb; Q9A0U7; -.
DR   PRIDE; Q9A0U7; -.
DR   EnsemblBacteria; AAK33584; AAK33584; SPy_0608.
DR   EnsemblBacteria; AAZ51123; AAZ51123; M5005_Spy0505.
DR   GeneID; 900815; -.
DR   KEGG; spy:SPy_0608; -.
DR   KEGG; spz:M5005_Spy0505; -.
DR   PATRIC; fig|160490.10.peg.520; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   Proteomes; UP000000750; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
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; Complete proteome; Lyase; Magnesium.
FT   CHAIN         1    920       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000166632.
FT   ACT_SITE    138    138       {ECO:0000255|HAMAP-Rule:MF_00595}.
FT   ACT_SITE    583    583       {ECO:0000255|HAMAP-Rule:MF_00595}.
FT   CONFLICT    859    859       D -> A (in Ref. 3; AAZ51123).
FT                                {ECO:0000305}.
SQ   SEQUENCE   920 AA;  104821 MW;  080B1F5D4C199237 CRC64;
     MPLKKLESSN NQDIIAEEVA LLKEMLENIT RRMIGDDAFT VIESIMVLSE KQDYIELEKV
     VANISNQEME VISRYFSILP LLINISEDVD LAYEINYQNN TDTDYLGKLA LTIKDLAGKD
     NGKDILEQVN VVPVLTAHPT QVQRKTILEL TTHIHKLLRK YRDAKAGVIN LEKWRQELYR
     YIEMIMQTDI IREKKLQVKN EIKNVMQYYD GSLIQAVTKL TTEYKNLAQK HGLELDNPKP
     ITMGMWIGGD RDGNPFVTAE TLCLSATVQS EVILNYYIDE 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 VADSNIIYRK LVFDNPHFYD
     YFFEASPIKE VSSLNIGSRP AARKTITEIT GLRAIPWVFS WSQNRIMFPG WYGVGSAFKR
     YIDRAQGNLE RLQHMYQTWP FFHSLLSNVD MVLSKSNMNI AFQYAQLAER QDVRDVFYEI
     LDEWQLTKNV ILAIQDHDDL LEDNPSLKHS LKSRLPYFNV LNYIQIELIK RWRNNQLDEN
     DEKLIHTTIN GIATGLRNSG
//
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