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Database: UniProt/TrEMBL
Entry: A4FM83_SACEN
LinkDB: A4FM83_SACEN
Original site: A4FM83_SACEN 
ID   A4FM83_SACEN            Unreviewed;       465 AA.
AC   A4FM83;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   11-MAY-2016, entry version 65.
DE   SubName: Full=Glutathione reductase {ECO:0000313|EMBL:CAM05158.1};
DE            EC=1.8.1.7 {ECO:0000313|EMBL:CAM05158.1};
GN   Name=mtr {ECO:0000313|EMBL:CAM05158.1};
GN   OrderedLocusNames=SACE_5978 {ECO:0000313|EMBL:CAM05158.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM05158.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAM05158.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|RuleBase:RU003691}.
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DR   EMBL; AM420293; CAM05158.1; -; Genomic_DNA.
DR   RefSeq; WP_009943708.1; NZ_ABFV01000009.1.
DR   ProteinModelPortal; A4FM83; -.
DR   STRING; 405948.SeryN2_010100006702; -.
DR   EnsemblBacteria; CAM05158; CAM05158; SACE_5978.
DR   KEGG; sen:SACE_5978; -.
DR   PATRIC; 23419324; VBISacEry28377_5952.
DR   eggNOG; ENOG4107QQC; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276709; -.
DR   KO; K17883; -.
DR   OMA; RGSAMKA; -.
DR   OrthoDB; EOG6QCD6D; -.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 3.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR017817; Mycothione_reductase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR03452; mycothione_red; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728};
KW   FAD {ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003691};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003691,
KW   ECO:0000313|EMBL:CAM05158.1};
KW   Redox-active center {ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN        4    324       FAD/NAD-binding_dom. {ECO:0000259|Pfam:
FT                                PF07992}.
FT   DOMAIN      349    458       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
SQ   SEQUENCE   465 AA;  50514 MW;  2FF3E39320176FC5 CRC64;
     MRHFDLVIIG SGSGNSILDD RFADWNVAIV EKGVGSTGNY GGTCLNVGCI PTKMFVHTAD
     VAGAPSSGTR LGVDLELRDV RWHDIRDRIF GRIDEISAGG RRYRAEDNPN VTLFEGVGRF
     TDVKRLEVET AGGTETITAD RFVVAAGGRP AIPDIPGIEN VDYHTSDSVM RLDELPRRMI
     IMGTGFVGAE FAHVFSALGV EVTLVGRSGR ALRSQDVDVS ERFTELAGRR WDLRLNRKEI
     GVEQDGDLTR LYLEGPDGSE VVEAEALLIA VGRVPNSDVL DAAKGGLALS RNGKIEVDSE
     QRTSVDGVWA LGDISSPYEL KHVANHEMRV VQHNLLHPDA PIESDHRYVP AAVFSSPQIA
     SVGLTEQEAQ QLGVEYVTSV QDYGGIAYGW AMEDSTGFAK LLADPETGKL LGAHIIGPQA
     PTLLQPLIQA MQFGLDARTM ARGQYWIHPG MPELIENALL NLPLR
//
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