ID A0A1X9LW57_9MICO Unreviewed; 458 AA.
AC A0A1X9LW57;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-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=B5808_19250 {ECO:0000313|EMBL:ARJ07539.1}, GCM10010988_39280
GN {ECO:0000313|EMBL:GGI42488.1};
OS Cnuibacter physcomitrellae.
OG Plasmid unnamed1 {ECO:0000313|EMBL:ARJ07539.1}.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cnuibacter.
OX NCBI_TaxID=1619308 {ECO:0000313|EMBL:ARJ07539.1, ECO:0000313|Proteomes:UP000192775};
RN [1] {ECO:0000313|EMBL:ARJ07539.1, ECO:0000313|Proteomes:UP000192775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XA {ECO:0000313|EMBL:ARJ07539.1}, and XA(T)
RC {ECO:0000313|Proteomes:UP000192775};
RC PLASMID=Plasmid unnamed1 {ECO:0000313|Proteomes:UP000192775}, and
RC unnamed1 {ECO:0000313|EMBL:ARJ07539.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GGI42488.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15041 {ECO:0000313|EMBL:GGI42488.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GGI42488.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15041 {ECO:0000313|EMBL:GGI42488.1};
RA Sun Q., Zhou Y.;
RL Submitted (DEC-2022) 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}.
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DR EMBL; CP020716; ARJ07539.1; -; Genomic_DNA.
DR EMBL; BMHD01000003; GGI42488.1; -; Genomic_DNA.
DR RefSeq; WP_071044826.1; NZ_CP020716.1.
DR AlphaFoldDB; A0A1X9LW57; -.
DR KEGG; cphy:B5808_19250; -.
DR Proteomes; UP000192775; Plasmid unnamed1.
DR Proteomes; UP000633908; 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: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.
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}; Plasmid {ECO:0000313|EMBL:ARJ07539.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000192775}.
FT DOMAIN 7..317
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 337..442
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 178..185
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 44..49
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 458 AA; 47519 MW; F9DC44D7C6A294F9 CRC64;
MTQHNEFDLA VVGTGGAAMS AAIHARLEGA SVVAIESGTL GGTCVNVGCV PSKTLLAAAH
TRHAALTNPF PGAATSAGAV DLGALVQQKD ELVGMLRQTK YADIAAAYGF DILPGTATFT
DPSTLLVDGR PVRAKSYLIA TGAEPTIPTI PGLEQIDYLT STTAMELTEL PASLVVIGGG
FVGLEQAQLF ARLGVEVTII GRLAPHAEPE LSSELRKAFL TDGITVIGDR AATITPHDDL
VRVLTRTGKV ATGERVLVAT GRTPRTDGLG LATAGIATDT RGFIIVDEQQ RTTNPAVFAA
GDVTDVPQYV YVAARTGKIA AHNALGHSEQ VDYTGLPSVL FTSPQLASAG ITEAEAIAAG
YRCACRYLRL ADVPRAIANH NTRGGIKIVA DADTGKVLGV HALADTAGEM MLAATYAIKA
GFTVTQLADT WAPYLTMAEG IRLTANLFRN ELPTSCCA
//
