ID A0A3G8JMT1_9ACTN Unreviewed; 498 AA.
AC A0A3G8JMT1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Mercuric reductase {ECO:0000313|EMBL:AZG46377.1};
DE EC=1.16.1.1 {ECO:0000313|EMBL:AZG46377.1};
GN Name=merA {ECO:0000313|EMBL:AZG46377.1};
GN ORFNames=D7316_02978 {ECO:0000313|EMBL:AZG46377.1};
OS Gordonia insulae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=2420509 {ECO:0000313|EMBL:AZG46377.1, ECO:0000313|Proteomes:UP000271469};
RN [1] {ECO:0000313|EMBL:AZG46377.1, ECO:0000313|Proteomes:UP000271469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS17-SY073 {ECO:0000313|EMBL:AZG46377.1,
RC ECO:0000313|Proteomes:UP000271469};
RA Kim Y.S., Kim S.B.;
RT "Gordonia insulae sp. nov., isolated from an island soil.";
RL Submitted (NOV-2018) 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; CP033972; AZG46377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G8JMT1; -.
DR KEGG; gom:D7316_02978; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000271469; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016152; F:mercury (II) reductase activity; IEA:UniProtKB-EC.
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; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 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|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000313|EMBL:AZG46377.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000271469}.
FT DOMAIN 10..355
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 385..490
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 121
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 161..163
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 198..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 48..53
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 498 AA; 52032 MW; 36634D43CB3DF6A8 CRC64;
MTGATDISTY DVVVIGGGPV GENAADYAIR GSDRTAAIIE HELVGGECSY WACMPSKGLL
GPGAALAAAA GLPGAREQLS NPTPDVTAVL GWRDTITHRR DDSSQVDWAS GAGIEVIRGH
GRIVGEREVA VGDGGESGRG ERSDGGFDRR IVAREAVVVA TGSTASVPPI PGLREARPWT
SRDATNMVEV PERMVVLGGG VVACEAVTWL LDLGVRDLTM VIRGDRLLPK AEPFVGEQVA
TGLARRGVDI RFGAQISAVE RPDVADTGYG HIHGGPARVT VDEGAGSSVL DVDEILVAAG
RSPATTDLGL DVLGIESTGP LRVDDHMGVP GHPWLYAVGD VNGRVALTHM GKYQGRVAGD
VIAARAEGHP LDGARFTASA DRDAIPQVVF TRPEMASVGR TEAQARDDGI DVVIAETDIA
VAGSYLVSPD YAGHAKLVID RSRDVLVGAT FVGAETAELV HSATVAVVGE VTVDRLWHAV
PSYPTVSEVW LRLLESLR
//
