(data stored in ACNUC7421 zone)

SWISSPROT: B4SID2_STRM5

ID   B4SID2_STRM5            Unreviewed;       262 AA.
AC   B4SID2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   SubName: Full=Extradiol ring-cleavage dioxygenase class III protein subunit B {ECO:0000313|EMBL:ACF50137.1};
GN   OrderedLocusNames=Smal_0432 {ECO:0000313|EMBL:ACF50137.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50137.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50137.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50137.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001111; ACF50137.1; -; Genomic_DNA.
DR   RefSeq; WP_012509928.1; NC_011071.1.
DR   STRING; 391008.Smal_0432; -.
DR   EnsemblBacteria; ACF50137; ACF50137; Smal_0432.
DR   KEGG; smt:Smal_0432; -.
DR   eggNOG; ENOG4105C8E; Bacteria.
DR   eggNOG; COG3384; LUCA.
DR   HOGENOM; HOG000236849; -.
DR   KO; K15777; -.
DR   OMA; WMGLAKR; -.
DR   OrthoDB; 1728007at2; -.
DR   BioCyc; SMAL391008:SMAL_RS02225-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   CDD; cd07363; 45_DOPA_Dioxygenase; 1.
DR   InterPro; IPR014436; Extradiol_dOase_DODA.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   Pfam; PF02900; LigB; 1.
DR   PIRSF; PIRSF006157; Doxgns_DODA; 1.
PE   4: Predicted;
DR   PRODOM; B4SID2.
DR   SWISS-2DPAGE; B4SID2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Dioxygenase {ECO:0000313|EMBL:ACF50137.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ACF50137.1}.
FT   DOMAIN        6    235       LigB. {ECO:0000259|Pfam:PF02900}.
SQ   SEQUENCE   262 AA;  28365 MW;  F8BAE84BF1D3070E CRC64;
     MSRLPSLYIS HGSPMTALHP GQVGVRLAEL ARDLPAPRAI VMASAHWLGR QPLVGAHPQP
     PTIHDFGGFP RALFELQYPA PGDPALAEEV AGRIAAAGLP VALDPQRGLD HGAWVPLRLL
     RPQADIPVVP VSIQPLLGPE HQFALGRALA PLREQGVLLV GSGSITHNLH DWGDYQDGKE
     APYVRPFIEW VEQRLAANDR QALLDYRRQA PFAERAHPTD EHLLPLFFAM GAAGEGGFGA
     RRIDAGIDAG FLAMDLYRFD GA
//

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