ID   A0A399SJE4_9BACT        Unreviewed;       464 AA.
AC   A0A399SJE4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Mercuric reductase {ECO:0000313|EMBL:RIJ43029.1};
GN   ORFNames=D1627_04115 {ECO:0000313|EMBL:RIJ43029.1};
OS   Pontibacter oryzae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=2304593 {ECO:0000313|EMBL:RIJ43029.1, ECO:0000313|Proteomes:UP000266005};
RN   [1] {ECO:0000313|Proteomes:UP000266005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIRAN {ECO:0000313|Proteomes:UP000266005};
RA   Seo T.;
RT   "Mucilaginibacter sp. MYSH2.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RIJ43029.1}.
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DR   EMBL; QWGE01000001; RIJ43029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399SJE4; -.
DR   OrthoDB; 9800167at2; -.
DR   Proteomes; UP000266005; 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; 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          10..326
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          350..457
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        448
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         54
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         183..190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         274
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         315
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        45..50
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   464 AA;  50454 MW;  9A3C50981FE3E19F CRC64;
     MENTQEHFSA IIIGTGQAGT PLAKALAKTG QQVAIIEASY VGGSCINYGC TPTKTLLASA
     KAAHTARQSA DFGVHTGKIS VEMQEVKARR DKVVQQFREG TEAGLDVENL TFIAGKAVFQ
     NAHTLQVNLN DGGTRTITGD KIFVNTGAIP NIPPLDGLDK IDYLTHISIQ ELTEVPEHLV
     ILGGGYVGLE FGQMYRRFGS QVTIVQRGEQ LLEREDEDVA QCLQHILEDE GIRVLLQTEA
     QCINKTNGQL QLDVKLQNGQ TETIGASHLL IATGVKAATE NLGLDKAGVE TDEKGNIETN
     ASLQTSVPHI YALGDVKGGP QFTHISFDDY RILRDNLLHN GQRTTTDRQV PYCVFTDPQL
     GRIGLTEKEA KEKGIPYKVA TLPMEKIARG IETGQTKGFY KALVHPETKV ILGAAILAPE
     GGEVMTMLEI AMMGNLKYTQ LKQGVFAHPT YGESLNNLFM KLED
//