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   27-MAR-2024, entry version 124.
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; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN 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-expression of
RT   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., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; NZ_VNID01000013.1.
DR   AlphaFoldDB; Q9RNU9; -.
DR   SMR; Q9RNU9; -.
DR   STRING; 100226.gene:17760744; -.
DR   PaxDb; 100226-SCO3127; -.
DR   PATRIC; fig|100226.15.peg.3191; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   InParanoid; Q9RNU9; -.
DR   OrthoDB; 9768133at2; -.
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   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   1: Evidence at protein level;
KW   Carbon dioxide fixation; Direct protein sequencing; Lyase; Magnesium;
KW   Reference proteome.
FT   CHAIN           1..911
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166628"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        569
FT                   /evidence="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
//