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Database: UniProt/SWISS-PROT
Entry: CAPP_STRR6
LinkDB: CAPP_STRR6
Original site: CAPP_STRR6 
ID   CAPP_STRR6              Reviewed;         898 AA.
AC   Q8DPW5;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   20-JUN-2018, entry version 81.
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=spr0974;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E.,
RA   LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P.,
RA   McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I.,
RA   Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P.,
RA   Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G.,
RA   Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L.,
RA   Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
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}.
DR   EMBL; AE007317; AAK99778.1; -; Genomic_DNA.
DR   PIR; F97993; F97993.
DR   RefSeq; NP_358568.1; NC_003098.1.
DR   RefSeq; WP_000058147.1; NC_003098.1.
DR   ProteinModelPortal; Q8DPW5; -.
DR   SMR; Q8DPW5; -.
DR   STRING; 171101.spr0974; -.
DR   PRIDE; Q8DPW5; -.
DR   EnsemblBacteria; AAK99778; AAK99778; spr0974.
DR   GeneID; 932953; -.
DR   KEGG; spr:spr0974; -.
DR   PATRIC; fig|171101.6.peg.1060; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   BioCyc; SPNE171101:SPR0974-MONOMER; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN         1    898       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000166631.
FT   ACT_SITE    138    138       {ECO:0000255|HAMAP-Rule:MF_00595}.
FT   ACT_SITE    561    561       {ECO:0000255|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   898 AA;  103209 MW;  DCDBCE2630E90ED0 CRC64;
     MSLQKLENSS NKSVVQEEVL ILTELLEDIT KNMLAPETFE KIIQLKELST QEDYQGLNRL
     VTSLSNDEMV YISRYFSILP LLINISEDVD LAYEINHQNN IDQDYLGKLS TTIKLVAEKE
     NAVEILEHLN VVPVLTAHPT QVQRKSMLDL TNHIHSLLRK YRDVKLGLIN KDKWYNDLRR
     YIEIIMQTDM IREKKLKVTN EITNAMEYYN SSFLKAVPHL TTEYKRLAQA HGLNLKQAKP
     ITMGMWIGGD RDGNPFVTAK 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 RSYDIYRDLV FGNEHFYDYF FESSPIKAIS SFNIGSRPAA
     RKTITEIGGL RAIPWVFSWS QSRVMFPGWY GVGSSFKEFI NKNPENIAIL RDMYQNWPFF
     QSLLSNVDMV LSKSNMNIAF EYAKLCEDEQ VKAIYETILN EWQVTKNVIL AIEGHDELLA
     DNPYLKASLD YRMPYFNILN YIQLELIKRQ RRGELSSDQE RLIHITINGI ATGLRNSG
//
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