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Database: UniProt
Entry: A0A0P0C6U6_9BACT
LinkDB: A0A0P0C6U6_9BACT
Original site: A0A0P0C6U6_9BACT 
ID   A0A0P0C6U6_9BACT        Unreviewed;       462 AA.
AC   A0A0P0C6U6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Mercuric reductase {ECO:0000313|EMBL:ALJ00996.1};
GN   ORFNames=DC20_20890 {ECO:0000313|EMBL:ALJ00996.1};
OS   Rufibacter tibetensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Rufibacter.
OX   NCBI_TaxID=512763 {ECO:0000313|EMBL:ALJ00996.1, ECO:0000313|Proteomes:UP000061382};
RN   [1] {ECO:0000313|EMBL:ALJ00996.1, ECO:0000313|Proteomes:UP000061382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1351 {ECO:0000313|EMBL:ALJ00996.1,
RC   ECO:0000313|Proteomes:UP000061382};
RA   Dai J.;
RT   "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT   radiation-resistant bacterium from tibet plateau.";
RL   Submitted (AUG-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; CP012643; ALJ00996.1; -; Genomic_DNA.
DR   RefSeq; WP_062545631.1; NZ_CP012643.1.
DR   AlphaFoldDB; A0A0P0C6U6; -.
DR   STRING; 512763.DC20_20890; -.
DR   KEGG; rti:DC20_20890; -.
DR   PATRIC; fig|512763.3.peg.4592; -.
DR   OrthoDB; 9800167at2; -.
DR   Proteomes; UP000061382; 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: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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061382}.
FT   DOMAIN          5..322
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          346..453
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        444
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         50
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         180..187
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         311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        41..46
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   462 AA;  50604 MW;  15CCB9C6E10B71BA CRC64;
     MKQYEAIIIG SGQGGTPLAM KLAQQGWNVA LVEKQYAGGT CVNVGCTPTK TMIASAKVAY
     TVAQAGKWGV EVNDFKLHLP AVLERKRKVV ESFRQGSEKG MEETENLCFI RGEASFIDRK
     TLRVTLKDGG EETLSANKIF IDVGTRAALP DVAGLRETDY LTSTTLLELE EVPERLIILG
     GGYIGLEFGQ MYRRFGSQVT ILDHNQRLLP REDEDIAAEV LKFLEAEGIQ VITGAQTTKV
     QKEGKYLNVT LKIGDEERII TGSHILVSAG RTPNTDTLNL PAAGVELDKR GYIKANDRLE
     TSAPGIYAIG DVKGGPAFTH ISYNDYLILY ENLVEGKNDS IQNRMVPYTM FTDPQLGRVG
     ITEQEARKSN LNIKVATLPM AHVARAIEIG DTRGMMKAIV DAGTGKILGV AIVGQEGGEV
     MSVLQMAMVG NVTWRQIKDM VFAHPLYAES LNTLFMKLEK EE
//
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