GenomeNet

Database: UniProt
Entry: A0A1M4WSG1_9GAMM
LinkDB: A0A1M4WSG1_9GAMM
Original site: A0A1M4WSG1_9GAMM 
ID   A0A1M4WSG1_9GAMM        Unreviewed;       479 AA.
AC   A0A1M4WSG1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Mercuric reductase {ECO:0000256|ARBA:ARBA00014791};
DE            EC=1.16.1.1 {ECO:0000256|ARBA:ARBA00012661};
DE   AltName: Full=Hg(II) reductase {ECO:0000256|ARBA:ARBA00031725};
GN   ORFNames=SAMN02745204_01236 {ECO:0000313|EMBL:SHE83983.1};
OS   Thermomonas hydrothermalis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Thermomonas.
OX   NCBI_TaxID=213588 {ECO:0000313|EMBL:SHE83983.1, ECO:0000313|Proteomes:UP000242857};
RN   [1] {ECO:0000313|Proteomes:UP000242857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14834 {ECO:0000313|Proteomes:UP000242857};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + Hg + NADP(+) = Hg(2+) + NADPH; Xref=Rhea:RHEA:23856,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16170, ChEBI:CHEBI:16793,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000896};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQUK01000017; SHE83983.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M4WSG1; -.
DR   STRING; 213588.SAMN02745204_01236; -.
DR   Proteomes; UP000242857; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016152; F:mercury (II) reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045340; F:mercury ion binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   GO; GO:0050787; P:detoxification of mercury ion; 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; IPR021179; Mercury_reductase_MerA.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   NCBIfam; TIGR02053; MerA; 1.
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; PR00945; HGRDTASE.
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   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:UP000242857}.
FT   DOMAIN          18..336
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          355..463
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   BINDING         63
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         195..202
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         280
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         321
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        54..59
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   479 AA;  50326 MW;  195521AC9A38D108 CRC64;
     MHPCCATTPH SAQEHTPRLA IIGSGGAAMA AALKAVERGA RVTLIERGTI GGTCVNVGCV
     PSKIMLRAAH IAYLRRESPF DGGVSATTPV IDRASLLAQQ QARVDELRHA KYEGILDGNP
     AITVLHGAAR FQDGRTLVVS LNEGGERTVA FDRCLIATGA SPAVPPIPGL KETPYWTSTE
     ALMSDAIPPR LAVIGSSVVA LELAQAFARL GSKVTILARS TLLFREDPAI GEAITNAFRA
     EGIEVLEHTQ ANQVAHTNGE FVLTTGHGEL RADQLLVATG RTPNTRDLDL EAAGVATNTQ
     GAIAVDSHLR TSAQDIYAAG DCTDLPQFVY VAAAAGTRAA INMTGGEATL DLTAMPAVVF
     TDPQVATVGL NEQEAHRAGI ETDSRTLTLD NVPRALTNFD TRGFIKLVTD AGSGRLIGVQ
     AVAPEAGELI QTAALAIRNR MTVQELADQL FPYLTMVEGL KLAAQTFSKD VKQLSCCAG
//
DBGET integrated database retrieval system