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Database: UniProt
Entry: E3E7Y8_PAEPS
LinkDB: E3E7Y8_PAEPS
Original site: E3E7Y8_PAEPS 
ID   E3E7Y8_PAEPS            Unreviewed;       403 AA.
AC   E3E7Y8;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   07-NOV-2018, entry version 47.
DE   SubName: Full=2,3-diketo-5-methylthiopentyl-1-phosphate enolase {ECO:0000313|EMBL:ADO57021.1};
GN   Name=ykrW {ECO:0000313|EMBL:ADO57021.1};
GN   ORFNames=PPSC2_14325 {ECO:0000313|EMBL:ADO57021.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO57021.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO57021.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO57021.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J.,
RA   Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of
RT   plant growth-promoting Rhizobacterium with broad-spectrum
RT   antimicrobial activity.";
RL   J. Bacteriol. 193:311-312(2011).
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC       {ECO:0000256|RuleBase:RU003834}.
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DR   EMBL; CP002213; ADO57021.1; -; Genomic_DNA.
DR   RefSeq; WP_013371620.1; NC_014622.2.
DR   ProteinModelPortal; E3E7Y8; -.
DR   STRING; 886882.PPSC2_c3061; -.
DR   EnsemblBacteria; ADO57021; ADO57021; PPSC2_14325.
DR   GeneID; 25387502; -.
DR   KEGG; ppm:PPSC2_14325; -.
DR   PATRIC; fig|886882.15.peg.3058; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230832; -.
DR   KO; K08965; -.
DR   OMA; FTQDWAS; -.
DR   OrthoDB; POG091H0DKL; -.
DR   BioCyc; PPOL886882:PPSC2_RS43045-MONOMER; -.
DR   Proteomes; UP000006868; Chromosome.
DR   GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:InterPro.
DR   CDD; cd08209; RLP_DK-MTP-1-P-enolase; 1.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   InterPro; IPR017717; Diketo-Methiopentyl-P_enolase.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   PANTHER; PTHR42704; PTHR42704; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDF00157; 2_3-diketo-5-methylthiopentyl-; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   TIGRFAMs; TIGR03332; salvage_mtnW; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006868};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT   DOMAIN        5    103       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      119    399       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
SQ   SEQUENCE   403 AA;  43358 MW;  CF37D9F237760149 CRC64;
     MSYCLATYRI YDDKADFNQK AQSIAIGMTV GSWTELPQAK RDAMQKHLGS VQSVDIHDGG
     PGERYADLTI AYPDVNFSRD IPALLVTVFG KISMDGRIKL MKLGFSEAFL SAFSGPKFGI
     SGLREQLGVY DRPLLMSIFK SVIGLNLEEL REQFTRQALG GVDLIKDDEI LFENALTPIE
     KRVEACIRAA EEAERETGKK LLYAANLTGP TSQLRAQALK AIDAGANALL FNVLAYGYDV
     LHELSSDPAV SVPIAAHPSL AGAAYPSPHY GISASVLLGQ LMRLAGADLV LFPSPYGSVT
     MPREENMAIR DELITPDSPL KACMPVPSAG IHPGLVPLIV RDFGTDVVVN AGGGIHGHPL
     GTEAGGRAFV QAIEAVQQNV PLAQYARTHP ELQSALDTWG GER
//
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