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Database: UniProt/TrEMBL
Entry: W0PD09_9BURK
LinkDB: W0PD09_9BURK
Original site: W0PD09_9BURK 
ID   W0PD09_9BURK            Unreviewed;       424 AA.
AC   W0PD09;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   25-OCT-2017, entry version 19.
DE   SubName: Full=Ribulose bisphosphate carboxylase {ECO:0000313|EMBL:AHG62918.1};
DE            EC=4.1.1.39 {ECO:0000313|EMBL:AHG62918.1};
GN   ORFNames=MIM_c08190 {ECO:0000313|EMBL:AHG62918.1};
OS   Advenella mimigardefordensis DPN7.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae.
OX   NCBI_TaxID=1247726 {ECO:0000313|EMBL:AHG62918.1, ECO:0000313|Proteomes:UP000019095};
RN   [1] {ECO:0000313|EMBL:AHG62918.1, ECO:0000313|Proteomes:UP000019095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPN7 {ECO:0000313|EMBL:AHG62918.1,
RC   ECO:0000313|Proteomes:UP000019095};
RX   PubMed=24739217; DOI=10.1099/mic.0.078279-0;
RA   Wubbeler J.H., Hiessl S., Schuldes J., Thurmer A., Daniel R.,
RA   Steinbuchel A.;
RT   "Unravelling the complete genome sequence of Advenella
RT   mimigardefordensis strain DPN7T and novel insights in the catabolism
RT   of the xenobiotic polythioester precursor 3,3'-dithiodipropionate.";
RL   Microbiology 160:1401-1416(2014).
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family.
CC       {ECO:0000256|RuleBase:RU003834}.
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DR   EMBL; CP003915; AHG62918.1; -; Genomic_DNA.
DR   RefSeq; WP_025371524.1; NZ_CP003915.1.
DR   ProteinModelPortal; W0PD09; -.
DR   EnsemblBacteria; AHG62918; AHG62918; MIM_c08190.
DR   KEGG; amim:MIM_c08190; -.
DR   PATRIC; fig|1247726.3.peg.887; -.
DR   KO; K01601; -.
DR   Proteomes; UP000019095; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
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   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SUPFAM; SSF51649; SSF51649; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000019095};
KW   Lyase {ECO:0000313|EMBL:AHG62918.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019095}.
FT   DOMAIN       14    129       RuBisCO_large_N. {ECO:0000259|Pfam:
FT                                PF02788}.
FT   DOMAIN      139    419       RuBisCO_large. {ECO:0000259|Pfam:
FT                                PF00016}.
SQ   SEQUENCE   424 AA;  45449 MW;  36FE1AD8D466A28F CRC64;
     MSDTAVQARY VIETPFDPAK VAEIMAGEQS CGTFTRVAGE TDELRDRARA TVTAIEALPA
     GEVPSLPNAW LERRNVRGPW RRALIDISFP IANIGANLAT LAATVSGNLY DLGEVTGLRL
     ESLTLPASYR MRFALPRVGI SGTRASIGVT AGAMVGTIIK PNVGMSAVQT AALVKTLCEA
     GVDFIKDDEV CANPEHAPLA ERVPAVMAVI RNHAQRTGKK VMMAFNISDD LDAMRRHAEL
     VAQEEGTCVM ASLNYCGFSA IESLRKSTPL AIHGHRNGFG AISRHPFLGM AYQPYQTMWR
     LAGVDHMHVH GLQGKFSQPD SEVVSAASDS LANMSDTVDD RVLPVFSSGQ WAGTVPATWQ
     SIQSQDLLFM SGGGILAHPM GPAAGVVSLR QAWAAQRQGV TLDDYARDMP ELQSALAFFG
     GRQS
//
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