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Database: UniProt
Entry: A0A0F4IYB6_9ACTN
LinkDB: A0A0F4IYB6_9ACTN
Original site: A0A0F4IYB6_9ACTN 
ID   A0A0F4IYB6_9ACTN        Unreviewed;       335 AA.
AC   A0A0F4IYB6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KJY26659.1};
DE   Flags: Fragment;
GN   ORFNames=VR44_29525 {ECO:0000313|EMBL:KJY26659.1};
OS   Streptomyces katrae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY26659.1, ECO:0000313|Proteomes:UP000033551};
RN   [1] {ECO:0000313|EMBL:KJY26659.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY26659.1};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) 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:KJY26659.1}.
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DR   EMBL; JZWV01000913; KJY26659.1; -; Genomic_DNA.
DR   RefSeq; WP_045950676.1; NZ_JZWV01000913.1.
DR   AlphaFoldDB; A0A0F4IYB6; -.
DR   PATRIC; fig|68223.7.peg.2278; -.
DR   OrthoDB; 3435382at2; -.
DR   Proteomes; UP000033551; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR   PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
FT   DOMAIN          1..187
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          221..326
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KJY26659.1"
SQ   SEQUENCE   335 AA;  34498 MW;  F022C0F5AE43074D CRC64;
     GSEPVLPDID GLDGAGAWTS ERATTADAVP GRLVVIGGGV VACEAATAWR SLGAEVTVLV
     RGRSLLSDWE PCAGEEVARG LTGLGAAVRF GVTALSLARD ADTGEVSVET DDGGVLRCDE
     LLVAVGRRPR TAGLGLEDVV PGYPASAADR LPVDDTGRVT SVPGGWLYAI GDVSGRAQLT
     HLAKYQARAC AAALVERAAG RPAEGGPRQP WSAGAARTAA ARAVFTLPEL ASVGLTERAA
     RGAGFTVRTA EYRTDDVAGA ALHADGYRGH AKLVVDADRR VVLGCTLTGP MATELIHTAT
     VAIVGDVPLD RLWHAVPAFP TVGEVWLRLL EAYGL
//
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