GenomeNet

Database: UniProt/SWISS-PROT
Entry: CAPP_STRCO
LinkDB: CAPP_STRCO
Original site: CAPP_STRCO 
ID   CAPP_STRCO              Reviewed;         911 AA.
AC   Q9RNU9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   05-DEC-2018, entry version 107.
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=SCO3127;
GN   ORFNames=SCE66.06c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN
RP   SEQUENCE.
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=8328954; DOI=10.1042/bj2930131;
RA   Bramwell H., Nimmo H.G., Hunter I.S., Coggins J.R.;
RT   "Phosphoenolpyruvate carboxylase from Streptomyces coelicolor A3(2):
RT   purification of the enzyme, cloning of the ppc gene and over-
RT   expression of the protein in a streptomycete.";
RL   Biochem. J. 293:131-136(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RA   Ricketts A.D.J., Hunter I.S.;
RT   "The ppc gene of Streptomyces coelicolor A3(2).";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RA   Alves A.M.C.R., te Poele E., White J., Bibb M.J., Dijkhuizen L.;
RT   "Characterization of the phosphoenolpyruvate carboxylase gene from
RT   Streptomyces coelicolor A3(2) and a ppc gene disruption mutant.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
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:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702;
CC         EC=4.1.1.31; 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00595}.
DR   EMBL; AF177946; AAD53311.1; -; Genomic_DNA.
DR   EMBL; AF160253; AAM54458.1; -; Genomic_DNA.
DR   EMBL; AL939115; CAB95920.1; -; Genomic_DNA.
DR   RefSeq; NP_627344.1; NC_003888.3.
DR   RefSeq; WP_003975687.1; NC_003888.3.
DR   ProteinModelPortal; Q9RNU9; -.
DR   SMR; Q9RNU9; -.
DR   STRING; 100226.SCO3127; -.
DR   PRIDE; Q9RNU9; -.
DR   EnsemblBacteria; CAB95920; CAB95920; CAB95920.
DR   GeneID; 1098561; -.
DR   KEGG; sco:SCO3127; -.
DR   PATRIC; fig|100226.15.peg.3191; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   InParanoid; Q9RNU9; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   PhylomeDB; Q9RNU9; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Carbon dioxide fixation; Complete proteome; Direct protein sequencing;
KW   Lyase; Magnesium; Reference proteome.
FT   CHAIN         1    911       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000166628.
FT   ACT_SITE    137    137       {ECO:0000255|HAMAP-Rule:MF_00595}.
FT   ACT_SITE    569    569       {ECO:0000255|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   911 AA;  101297 MW;  5192E0BB96881273 CRC64;
     MSSADDQTTT TTSSELRADI RRLGDLLGET LVRQEGPELL ELVEKVRRLT REDGEAAAEL
     LRGTELETAA KLVRAFSTYF HLANVTEQVH RGRELGAKRA AEGGLLARTA DRLKDADPEH
     LRETVRNLNV RPVFTAHPTE AARRSVLNKL RRIAALLDTP VNESDRRRLD TRLAENIDLV
     WQTDELRVVR PEPADEARNA IYYLDELHLG AVGDVLEDLT AELERAGVKL PDDTRPLTFG
     TWIGGDRDGN PNVTPQVTWD VLILQHEHGI NDALEMIDEL RGFLSNSIRY AGATEELLAS
     LQADLERLPE ISPRYKRLNA EEPYRLKATC IRQKLENTKQ RLAKGTPHED GRDYLGTAQL
     IDDLRIVQTS LREHRGGLFA DGRLARTIRT LAAFGLQLAT MDVREHADAH HHALGQLFDR
     LGEESWRYAD MPREYRTKLL AKELRSRRPL APSPAPVDAP GEKTLGVFQT VRRALEVFGP
     EVIESYIISM CQGADDVFAA AVLAREAGLI DLHAGWAKIG IVPLLETTDE LKAADTILED
     LLADPSYRRL VALRGDVQEV MLGYSDSSKF GGITTSQWEI HRAQRRLRDV AHRYGVRLRL
     FHGRGGTVGR GGGPTHDAIL AQPWGTLEGE IKVTEQGEVI SDKYLIPALA RENLELTVAA
     TLQASALHTA PRQSDEALAR WDAAMDVVSD AAHTAYRHLV EDPDLPTYFL ASTPVDQLAD
     LHLGSRPSRR PGSGVSLDGL RAIPWVFGWT QSRQIVPGWY GVGSGLKALR EAGLDTVLDE
     MHQQWHFFRN FISNVEMTLA KTDLRIAQHY VDTLVPDELK HVFDTIKAEH ELTVAEVLRV
     TGESELLDAD PVLKQTFTIR DAYLDPISYL QVALLGRQRE AAAANEDPDP LLARALLLTV
     NGVAAGLRNT G
//
DBGET integrated database retrieval system