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Database: UniProt/SWISS-PROT
Entry: CAPP_STRAW
LinkDB: CAPP_STRAW
Original site: CAPP_STRAW 
ID   CAPP_STRAW              Reviewed;         910 AA.
AC   Q82HE3;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   10-OCT-2018, entry version 93.
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=SAV_3566;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 /
OS   NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C.,
RA   Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T.,
RA   Kikuchi H., Shiba T., Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces
RT   avermitilis: deducing the ability of producing secondary
RT   metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC71278.1; -; Genomic_DNA.
DR   RefSeq; WP_010984997.1; NZ_JZJK01000090.1.
DR   ProteinModelPortal; Q82HE3; -.
DR   SMR; Q82HE3; -.
DR   STRING; 227882.SAV_3566; -.
DR   EnsemblBacteria; BAC71278; BAC71278; SAVERM_3566.
DR   KEGG; sma:SAVERM_3566; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; SAVE227882:G1G23-3743-MONOMER; -.
DR   Proteomes; UP000000428; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Carbon dioxide fixation; Complete proteome; Lyase; Magnesium;
KW   Reference proteome.
FT   CHAIN         1    910       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000166627.
FT   ACT_SITE    136    136       {ECO:0000255|HAMAP-Rule:MF_00595}.
FT   ACT_SITE    568    568       {ECO:0000255|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   910 AA;  101200 MW;  D327E1B9D164403D CRC64;
     MSSADDQTTT TSSELRADIR RLGDLLGETL VRQEGPELLD LVEKVRRLTR EDGEAAAELL
     RGTELETAAK LVRAFSTYFH LANVTEQVHR GRELRTKRAA EGGLLARTAD RLKDADPEHL
     RATVKNLNVR PVFTAHPTEA ARRSVLNKLR RIAALLETPV IEADRRRYDT RLAENIDLVW
     QTDELRVVRP EPADEARNAI YYLDELHAGA VGDVLEDLTA ELERVGVQLP DDTRPLTFGT
     WIGGDRDGNP NVTPEVTWDV LILQHEHGIN DALELIDELR GFLSNSIRYT GATEELLTSL
     GTDLERLPEI SPRYKRLNAE EPYRLKATCI RQKLENTKQR LAKGTAHQPG RDYLGTGELL
     HDLKLIQTSL REHRGGLFAD GRMDRTIRTL AAFGLQLATM DVREHADAHH YALGQLFDRL
     GEESWRYADM PRDYRGKLLA KELRSRRPLA PSPAPLDAAG AKTLGVFHTV KRALAVFGPE
     VIESYIISMC QGADDVFAAA VLAREAGLLD LHAGWAKIGI VPLLETTDEL KAADTILEDM
     LSDPSYRRLV ALRGDVQEVM LGYSDSSKFG GITTSQWEIH RAQRRLRDVA HRYGVRLRLF
     HGRGGTVGRG GGPSHDAILA QPWGTLEGEI KVTEQGEVIS DKYLVPSLAR ENLELTVAAT
     LQASALHTAP RQSDEALARW DAAMDVVSDA AHSAYRRLVE DPDLPTYFLA STPVDQLADL
     HLGSRPSRRP GSGVSLDGLR AIPWVFGWTQ SRQIVPGWFG VGSGLKALRE AGLDTVLDEM
     HEQWHFFRNF LSNVEMTLAK TDLRIARHYV DTLVPDHLKH VFATIEAEHE LTVREVLRIT
     GGEKLLDTHP VLQQTFAIRD AYLDPISYLQ VALLKRQRDA AAADTPPDPL LARALLLTVN
     GVAAGLRNTG
//
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