ID   A0ZCZ5_NODSP            Unreviewed;       484 AA.
AC   A0ZCZ5;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   SubName: Full=Mercuric ion reductase {ECO:0000313|EMBL:AHJ28319.1};
DE            EC=1.16.1.1 {ECO:0000313|EMBL:AHJ28319.1};
GN   ORFNames=NSP_19860 {ECO:0000313|EMBL:AHJ28319.1};
OS   Nodularia spumigena CCY9414.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Nodularia.
OX   NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ28319.1, ECO:0000313|Proteomes:UP000019325};
RN   [1] {ECO:0000313|EMBL:AHJ28319.1, ECO:0000313|Proteomes:UP000019325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ28319.1};
RX   PubMed=23555932;
RA   Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA   Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA   Stal L.J., Hess W.R.;
RT   "Insights into the physiology and ecology of the brackish-water-adapted
RT   Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT   analysis.";
RL   PLoS ONE 8:E60224-E60224(2013).
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; CP007203; AHJ28319.1; -; Genomic_DNA.
DR   RefSeq; WP_006195347.1; NZ_CP007203.1.
DR   AlphaFoldDB; A0ZCZ5; -.
DR   STRING; 313624.NSP_19860; -.
DR   GeneID; 78016027; -.
DR   PATRIC; fig|313624.11.peg.2003; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_1_0_3; -.
DR   Proteomes; UP000019325; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016152; F:mercury (II) reductase activity; IEA:UniProtKB-EC.
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:SF2; MERCURIC REDUCTASE; 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};
KW   Oxidoreductase {ECO:0000313|EMBL:AHJ28319.1}.
FT   DOMAIN          5..321
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          344..453
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   BINDING         117
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         309
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ   SEQUENCE   484 AA;  53383 MW;  75CEAC1A1FDAEB4F CRC64;
     MTIDYDLVII GGTLAGRYAA LVATQLKATV ALVESQVNYE FSQHQAMSEI GNIVHNMNDV
     AGLGIHSTQA KNSDKCQVSV TWTEAKRYTD GVVSNIQEQN SPANLAALGV DVILGSGQFQ
     SLPHLAFAVN QRLLRGRTYL LASGSVRGVP DIEGLQTTGY LTLSNIWQCL KQPSLPQNWV
     IIGGVPQSIE VAQTLARLGC SVTLAVKSAS ILPYADSEIA HLLQAQLEVD GVRVLTQKPV
     TQVKLIEDKK WVQAGDKAIE TDEILVATDQ EPNVEFLNLA AVGVKWRQRR LVVNDKLQTT
     NHRIYACGDV IGGYDFPNVA NYEARIAVKN ALFFPRLRVN YQCIPWGLNS HPRLAEVGLT
     EAQAKRQFKL DEVFVLRQYY KSVTAAQLRD ETTGICKLIV LRNGEILGAS ILGAEAGELI
     NLIALAMSQK IRVKQLANLS AVYPSFSEII ENAAREWGKE KLNSNFGLQD FLEGLFHFRR
     DWNL
//