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Database: UniProt
Entry: A0A3N6FQW4_9ACTN
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ID   A0A3N6FQW4_9ACTN        Unreviewed;       410 AA.
AC   A0A3N6FQW4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Rhodocoxin reductase {ECO:0000313|EMBL:RPK74994.1};
DE            EC=1.18.1.- {ECO:0000313|EMBL:RPK74994.1};
GN   Name=thcD2 {ECO:0000313|EMBL:RPK74994.1};
GN   ORFNames=EES45_26040 {ECO:0000313|EMBL:RPK74994.1};
OS   Streptomyces sp. ADI97-07.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1522762 {ECO:0000313|EMBL:RPK74994.1, ECO:0000313|Proteomes:UP000281409};
RN   [1] {ECO:0000313|EMBL:RPK74994.1, ECO:0000313|Proteomes:UP000281409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ADI97-07 {ECO:0000313|EMBL:RPK74994.1,
RC   ECO:0000313|Proteomes:UP000281409};
RA   Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA   Busche T., Kalinowski J., Zotchev S.B.;
RT   "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT   secondary metabolite biosynthesis gene clusters and some of their
RT   products.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RPK74994.1}.
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DR   EMBL; RPGY01000134; RPK74994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N6FQW4; -.
DR   Proteomes; UP000281409; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:RPK74994.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281409}.
FT   DOMAIN          16..302
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          325..408
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   410 AA;  42681 MW;  ACE062C06A4B067E CRC64;
     MSEQTWDRTA GERPRRVVVV GAGMAGVQTA VALREQGFAG PVTLIGAEPH QPYDRPPLSK
     AVLLGKAEDS AFDVDFEALD ITLRLGLDVT GLRAAAHELD TPEGPVPYDV LVLATGAEPL
     VLPGSEGVPG VHLLRTLDDA ERLRPVLERQ HDVVVVGAGW IGAEFTTAAR AAGCAVTVIE
     AAGRPLAGTL PAEVAAPMAA WYAESGAELL TGARVARVEP GAVHLTDGRA VPAGAVIVGI
     GARPATGWLA GSGIALGPDG SVTADGSLRT SLPDVYAVGD CASFPSARYG ERLLVHHWDN
     ALQGPRAVAA AVADGLPRTY DPVPYFWSEQ FGRFVQYAGH HAGADTLLWR GDPAEAAWTV
     CWLRAGVLVA VLAVGRPRDL AQGRKLVEAG ARIDPVRAAD PSVPLRSAVL
//
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