ID A0A1V2H452_9PROT Unreviewed; 450 AA.
AC A0A1V2H452;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Mercuric reductase {ECO:0000313|EMBL:ONG55804.1};
GN ORFNames=BKE38_08440 {ECO:0000313|EMBL:ONG55804.1};
OS Pseudoroseomonas deserti.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=1817963 {ECO:0000313|EMBL:ONG55804.1, ECO:0000313|Proteomes:UP000188879};
RN [1] {ECO:0000313|EMBL:ONG55804.1, ECO:0000313|Proteomes:UP000188879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3 {ECO:0000313|EMBL:ONG55804.1,
RC ECO:0000313|Proteomes:UP000188879};
RA Subhash Y., Lee S.;
RT "Draft Genome sequence of Roseomonas sp. strain M3.";
RL Submitted (OCT-2016) 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,
CC ECO:0000256|RuleBase:RU003691}.
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:ONG55804.1}.
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DR EMBL; MLCO01000066; ONG55804.1; -; Genomic_DNA.
DR RefSeq; WP_076956908.1; NZ_MLCO01000066.1.
DR AlphaFoldDB; A0A1V2H452; -.
DR OrthoDB; 9764616at2; -.
DR Proteomes; UP000188879; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; 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 InterPro; IPR012999; Pyr_OxRdtase_I_AS.
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.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000188879}.
FT DOMAIN 5..315
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 340..444
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 435
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 174..181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 302
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 450 AA; 47071 MW; 84401D09620F7141 CRC64;
MTAFDSIVVG AGQAGPSLAV RLAEAGKKVA LVERSLLGGT CVNRGCMPTK ALVASARAAH
VARRAADWGI AVGGPVTAEM PRITARAQKV ASDARGNLQR WLEGVEGVAL VQGHARFTAP
FTLQVGQEVL TAPQIFLNVG ARAVVPDGFE GVPFLTSSSI LQITHLPRHL VILGGSYIGL
EFAQAYRRFG SAVTVLERGP KLLPREDADI SDEIRSILEA EGISVRCGVG DVAASADAGG
VTLGFGEGQS VSGSDLLIAV GRRPNTDELG LAMAGIAVDP RGFITVDERL QTNVPGVYAL
GDCNGRGAFT HTAYNDFEIV AANLLDGEDR RVSERVSGYA LYIDPPLGRV GMTEAAARGS
GLDVQVSTRP MSRVGRAVEK GETAGFMKVV AERDTGRILG AAILGVEGDE AIHGLLDAMH
AGVPQQVLRW AVPIHPTVSE LIPTLLQGLR
//
