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 25-MAY-2022, entry version 116.
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 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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00595}.
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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.SCO3127; -.
DR GeneID; 1098561; -.
DR KEGG; sco:SCO3127; -.
DR PATRIC; fig|100226.15.peg.3191; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_11; -.
DR InParanoid; Q9RNU9; -.
DR OMA; PWVFGWT; -.
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; 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
