ID A0A0K2M0Q2_9NOST Unreviewed; 485 AA.
AC A0A0K2M0Q2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Mercuric reductase {ECO:0000313|EMBL:ALB41640.1};
GN ORFNames=AA650_15275 {ECO:0000313|EMBL:ALB41640.1};
OS Anabaena sp. WA102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=1647413 {ECO:0000313|EMBL:ALB41640.1, ECO:0000313|Proteomes:UP000056652};
RN [1] {ECO:0000313|EMBL:ALB41640.1, ECO:0000313|Proteomes:UP000056652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA102 {ECO:0000313|EMBL:ALB41640.1,
RC ECO:0000313|Proteomes:UP000056652};
RA Brown N.M.;
RT "The finished genome of an anatoxin-a-producing Anabaena isolate reveals
RT extensive genome rearrangement.";
RL Submitted (MAY-2015) 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}.
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DR EMBL; CP011456; ALB41640.1; -; Genomic_DNA.
DR RefSeq; WP_053539639.1; NZ_CP011456.1.
DR AlphaFoldDB; A0A0K2M0Q2; -.
DR STRING; 1647413.AA650_15275; -.
DR KEGG; awa:AA650_15275; -.
DR PATRIC; fig|1647413.5.peg.3610; -.
DR OrthoDB; 501518at2; -.
DR Proteomes; UP000056652; 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:SF2; MERCURIC REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 2.
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 6..314
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 345..453
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 184..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 485 AA; 54785 MW; 320E1D70052D01DB CRC64;
MTNIDYDIVI IGGSIAGYQA ALSATQLHAK VALIVSADFT HNYNLNYQYI LSEISQTTQK
YYNLVNLGTY EKNIHLNLEF LNWKKGMFYA NAVAKNINQI HSLANLAAQG VDIIVGNGQF
QSSPQLSFTV NERRLYSRTY LLANGSRPLI PNISGLDTIK YLTLANIWQF LEKTTLPENW
VIIGGIPQSI EIAQVLARFG CQVTLIVKYS SILPSLDAEI AKLLTAQLEI DGVRILTQTQ
VTQVRQIDHK KWVQAGNQAI ETDEIFICAG QQPNLEYLNL PAVGVKWHQY RLVVNEKLQT
TNHRIYACGD VLGGYDIQNI GNYEANIAVK NALLFPKLKV NYEFVPWGIY SQPRVAQVGL
TEKQAKNQYS QKQVLVFKQY FKTATAAQIQ GEITGVCKLV VLENGKILGC SILGIAAEEL
INLISLAISQ NMKIQYLAKL SPIYPSFSEI LMEIAREWHR QRINQNHTFS ELLLSFFNYR
RDWNL
//
