ID   A0A094IPI6_9GAMM        Unreviewed;       197 AA.
AC   A0A094IPI6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Mercuric reductase {ECO:0000313|EMBL:KFZ27754.1};
DE   Flags: Fragment;
GN   ORFNames=IDAT_12985 {ECO:0000313|EMBL:KFZ27754.1};
OS   Pseudidiomarina atlantica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Pseudidiomarina.
OX   NCBI_TaxID=1517416 {ECO:0000313|EMBL:KFZ27754.1, ECO:0000313|Proteomes:UP000053718};
RN   [1] {ECO:0000313|EMBL:KFZ27754.1, ECO:0000313|Proteomes:UP000053718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A10513 {ECO:0000313|EMBL:KFZ27754.1,
RC   ECO:0000313|Proteomes:UP000053718};
RA   Du J., Lai Q., Shao Z.;
RT   "Draft genome sequence of Idiomarina sp. MCCC 1A10513.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KFZ27754.1}.
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DR   EMBL; JPIN01000038; KFZ27754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094IPI6; -.
DR   STRING; 1517416.IDAT_12985; -.
DR   eggNOG; COG1249; Bacteria.
DR   OrthoDB; 9800167at2; -.
DR   Proteomes; UP000053718; 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; 1.
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; 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          1..54
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          73..179
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFZ27754.1"
SQ   SEQUENCE   197 AA;  20679 MW;  E21012A9F799A283 CRC64;
     TPNTENLDLK TIGVQTERGT ITINERMQTS NSRVYAAGDC TNQPQFVYVA AAGGSRAAIN
     MTGGDAHLDL SAMPEVIFTD PQVATVGLSE ADAKTGGYVT ESRTLGLENV PRALVNFNTQ
     GFIKIVAESG SGRLLGVQVV AGEAGELIQA AVMAIRAGMT VNELADELFP YLTMVEGLKL
     CAQTFTKDVS QLSCCAG
//