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Database: UniProt/TrEMBL
Entry: E4WG82_RHOE1
LinkDB: E4WG82_RHOE1
Original site: E4WG82_RHOE1 
ID   E4WG82_RHOE1            Unreviewed;       458 AA.
AC   E4WG82;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   19-MAR-2014, entry version 20.
DE   SubName: Full=Mycothiol disulfide reductase Mtr;
GN   Name=mtr; OrderedLocusNames=REQ_18700;
OS   Rhodococcus equi (strain 103S) (Corynebacterium equi).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=685727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=103S;
RX   PubMed=20941392; DOI=10.1371/journal.pgen.1001145;
RA   Letek M., Gonzalez P., Macarthur I., Rodriguez H., Freeman T.C.,
RA   Valero-Rello A., Blanco M., Buckley T., Cherevach I., Fahey R.,
RA   Hapeshi A., Holdstock J., Leadon D., Navas J., Ocampo A., Quail M.A.,
RA   Sanders M., Scortti M.M., Prescott J.F., Fogarty U., Meijer W.G.,
RA   Parkhill J., Bentley S.D., Vazquez-Boland J.A.;
RT   "The genome of a pathogenic rhodococcus: cooptive virulence
RT   underpinned by key gene acquisitions.";
RL   PLoS Genet. 6:E1001145-E1001145(2010).
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DR   EMBL; FN563149; CBH47936.1; -; Genomic_DNA.
DR   RefSeq; YP_004006621.1; NC_014659.1.
DR   ProteinModelPortal; E4WG82; -.
DR   EnsemblBacteria; CBH47936; CBH47936; REQ_18700.
DR   GeneID; 9964630; -.
DR   KEGG; req:REQ_18700; -.
DR   PATRIC; 42661161; VBIRhoEqu141084_1871.
DR   HOGENOM; HOG000276709; -.
DR   KO; K17883; -.
DR   OMA; VKRVFGR; -.
DR   BioCyc; REQU685727:GHKP-1803-MONOMER; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR017817; Mycothione_reductase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR03452; mycothione_red; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   4: Predicted;
KW   Complete proteome.
SQ   SEQUENCE   458 AA;  49555 MW;  052D30DC68F14D7C CRC64;
     MNHFDLAIIG TGSGNSILDE RYDGKKVAIL EESTFGGTCL NVGCIPTKMF VYAAEVARTI
     TASSKLGIDA TLDDVRWSDI VKRVFGRIDP ISAGGERYRT EDCDNVTVFR GHARFVGPRS
     IDTGTGEVIT ADRVVIAAGS RPSIPNEVLE GGVRYHTNDD IMRLPELPER LVILGSGFIA
     AEFAHVFSAL GVQVSIVGRS DRLLRHLDKD VSTWFTELAQ RKWDVHLGNP MVAARPAGNG
     IELELADGTV VSGDELLVAV GRIPNGDRLD AALGGVAVDE AGRVIVDEYQ RTTAEGVFAL
     GDVSSPYQLK HVANHEMRVV QHNLLHDAWA STAHLRRTDH RFVPAAVFTD PQIADVGMTE
     EQAREAGLDI TVKLQNYCDV AYGWAMEDDE GFCKVIAERG TGRLLGAHVI GAQAPTVIQP
     LIQALSFGLS AQDMATGQYW IHPALPEVVE NALLGLDI
//
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