ID   F8SSB5_9GAMM            Unreviewed;       280 AA.
AC   F8SSB5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Mercury ion reductase {ECO:0000313|EMBL:AEI26145.1};
DE   Flags: Fragment;
GN   Name=merA {ECO:0000313|EMBL:AEI26145.1};
OS   Stenotrophomonas sp. C21O.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=999372 {ECO:0000313|EMBL:AEI26145.1};
RN   [1] {ECO:0000313|EMBL:AEI26145.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C21O {ECO:0000313|EMBL:AEI26145.1};
RA   Almeida B.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEI26145.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C21O {ECO:0000313|EMBL:AEI26145.1};
RA   Carvalho G., Fradinho J., Oehmen A., Reis M.A.M., Crespo T.B.;
RT   "Microbial characterisation of mercury reducing mixed cultures enriched
RT   with different carbon sources.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; HQ674978; AEI26145.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8SSB5; -.
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          2..180
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          199..280
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEI26145.1"
FT   NON_TER         280
FT                   /evidence="ECO:0000313|EMBL:AEI26145.1"
SQ   SEQUENCE   280 AA;  29275 MW;  AC8839AAD234B5E2 CRC64;
     SPAVPPIPGL KDTPYWTSTE ALVSETIPKR LAVIGSSVVA LELAQAFARL GAKVTILARS
     TLFFREDPAI GEAVTAAFRM EGIEVREHTQ ASQVAYINGE GDGEFVLTTA HGELRADKLL
     VATGRAPNTR KLALDATGVT LTPQGAIVID PGMRTSVEHI YAAGDCTDQP QFVYVAAAAG
     TRAAINMTGG DAALNLTAMP AVVFTDPQVA TVGYSEAEAH HDGIKTDSRT LTLDNVPRAL
     ANFDTRGFIK LVVEEGSGRL IGVQAVAPEA GELIQTAALA
//