ID A0A142YEX4_9PLAN Unreviewed; 464 AA.
AC A0A142YEX4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Mercuric reductase {ECO:0000313|EMBL:AMV37582.1};
DE EC=1.16.1.1 {ECO:0000313|EMBL:AMV37582.1};
GN Name=merA_1 {ECO:0000313|EMBL:AMV37582.1};
GN ORFNames=VT85_09105 {ECO:0000313|EMBL:AMV37582.1};
OS Planctomyces sp. SH-PL62.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctomyces.
OX NCBI_TaxID=1636152 {ECO:0000313|EMBL:AMV37582.1, ECO:0000313|Proteomes:UP000076365};
RN [1] {ECO:0000313|EMBL:AMV37582.1, ECO:0000313|Proteomes:UP000076365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL62 {ECO:0000313|EMBL:AMV37582.1,
RC ECO:0000313|Proteomes:UP000076365};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-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; CP011273; AMV37582.1; -; Genomic_DNA.
DR RefSeq; WP_068421693.1; NZ_CP011273.1.
DR AlphaFoldDB; A0A142YEX4; -.
DR STRING; 1636152.VT85_09105; -.
DR KEGG; plh:VT85_09105; -.
DR PATRIC; fig|1636152.3.peg.2080; -.
DR OrthoDB; 230580at2; -.
DR Proteomes; UP000076365; 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; 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 Oxidoreductase {ECO:0000313|EMBL:AMV37582.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076365}.
FT DOMAIN 9..328
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 350..454
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 448
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 184..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 45..50
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 464 AA; 50061 MW; 0D2E946862F114F5 CRC64;
MADRPEKFDA VLLGAGQANN PLSRSLARAG RRVALIEKGK IGGTCVNVGC TPTKTMAASA
RVAHLARRAR DFGVHTGPVA VRLQEVRART GAIVEEFSAG SERQLEEAEG VELIRGEGWF
TGPRTVRVEL NGGGVRELSG ELVVIDVGCR PARPEIPGLD SAPWLDSTRI LGLEATPDHL
LVLGGGYIGV EFAQMFRRFG SRVTLVQKGG QLLRREDPDM AEALAEILRE DGVEVILDAK
ATRVAGSAQE IRLTVEVDGR SRELTASHLM VATGRTPNTE SLNLTAAGVR TDDRGFIPVD
VRLETNVPGV YALGDVNGGP AFTHVSHNDN QILRENLLHD AGRTTAGRLV PFTVFTDPQF
GRVGLTEKEA RERGRRVRIA RLPMSQVARA LEIGESRGIL KAVVDAETDL ILGCTALAVE
GGEIMSMVQL AMMGGLPYQR LRDDMFSHPT LARGLNNLFA HLEE
//
