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Database: UniProt
Entry: W8VWA0_9FLAO
LinkDB: W8VWA0_9FLAO
Original site: W8VWA0_9FLAO 
ID   W8VWA0_9FLAO            Unreviewed;       445 AA.
AC   W8VWA0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Similar to glutathione reductase {ECO:0000313|EMBL:BAO54572.1};
GN   ORFNames=NMS_0563 {ECO:0000313|EMBL:BAO54572.1};
OS   Nonlabens marinus S1-08.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Nonlabens.
OX   NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO54572.1, ECO:0000313|Proteomes:UP000031760};
RN   [1] {ECO:0000313|EMBL:BAO54572.1, ECO:0000313|Proteomes:UP000031760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S1-08 {ECO:0000313|EMBL:BAO54572.1,
RC   ECO:0000313|Proteomes:UP000031760};
RX   PubMed=24706784; DOI=10.1073/pnas.1403051111;
RA   Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W.,
RA   DeLong E.F., Kogure K.;
RT   "Functional characterization of flavobacteria rhodopsins reveals a unique
RT   class of light-driven chloride pump in bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR   EMBL; AP014548; BAO54572.1; -; Genomic_DNA.
DR   AlphaFoldDB; W8VWA0; -.
DR   STRING; 1454201.NMS_0563; -.
DR   HOGENOM; CLU_016755_2_0_10; -.
DR   OrthoDB; 9800167at2; -.
DR   Proteomes; UP000031760; Chromosome.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
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   PIRSF; PIRSF000350; Mercury_reductase_MerA; 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   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DOMAIN          4..310
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          337..442
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   BINDING         50
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         112
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         171..178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         194
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         261
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         302
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        41..46
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   445 AA;  49111 MW;  9D7594F9F749D369 CRC64;
     MKHYDVFILG TGTAGKLVAN RCADAGLTVG IIDNREYGGT CSQRGCDPKK LMLASSEALE
     AARNMKGDGI TGDIAINWID VYNYARRYAQ DIPDNTEEFL KELGVDRHHG EGYFVDEKTF
     RYGDTSLTAD KFVIATGMKP LELKIPGAEH LLTSDDFFNL KDLPEKVLFI GGGYVGMEFS
     HMLARAGVKV TVVEQGEQLL PPFEKYTVDF LKECSEELGI DILLNSQAAA VEKDGDRFIV
     KYSKDGILHQ VTSDLIFNTA GRVPSIKQLQ LENAGVVTDR SGIVVNEYFQ STSNERFYAC
     GDVSSKNVPL TPLSGLEANI AAKNITEGKH AFIPVDIPSV AFTIPQVAGI GLTEKQAKAT
     GKKFKVFFQN ASGWFNTRRI KAGCYAYKVI VDEETRMVLG AHIISHEAGE TINIFSVAMN
     HDITFQYLQQ TIFTYPSWAN DIKSF
//
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