ID A0A1I7LGI4_9BACL Unreviewed; 554 AA.
AC A0A1I7LGI4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Mercuric reductase {ECO:0000256|ARBA:ARBA00014791, ECO:0000256|PIRNR:PIRNR000350};
DE EC=1.16.1.1 {ECO:0000256|ARBA:ARBA00012661, ECO:0000256|PIRNR:PIRNR000350};
DE AltName: Full=Hg(II) reductase {ECO:0000256|ARBA:ARBA00031725, ECO:0000256|PIRNR:PIRNR000350};
GN Name=merA {ECO:0000256|RuleBase:RU361223};
GN ORFNames=SAMN05421543_1481 {ECO:0000313|EMBL:SFV08780.1};
OS Alicyclobacillus macrosporangiidus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=392015 {ECO:0000313|EMBL:SFV08780.1, ECO:0000313|Proteomes:UP000183508};
RN [1] {ECO:0000313|Proteomes:UP000183508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17980 {ECO:0000313|Proteomes:UP000183508};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Resistance to Hg(2+) in bacteria appears to be governed by a
CC specialized system which includes mercuric reductase. MerA protein is
CC responsible for volatilizing mercury as Hg(0).
CC {ECO:0000256|PIRNR:PIRNR000350}.
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 ECO:0000256|PIRNR:PIRNR000350, ECO:0000256|RuleBase:RU361223};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR000350,
CC ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU361223};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRNR:PIRNR000350,
CC ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU361223};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|PIRNR:PIRNR000350, ECO:0000256|RuleBase:RU361223}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|PIRNR:PIRNR000350, ECO:0000256|RuleBase:RU361223}.
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DR EMBL; FPBV01000048; SFV08780.1; -; Genomic_DNA.
DR RefSeq; WP_074956733.1; NZ_FPBV01000048.1.
DR AlphaFoldDB; A0A1I7LGI4; -.
DR STRING; 392015.SAMN05421543_1481; -.
DR eggNOG; COG1249; Bacteria.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000183508; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016152; F:mercury (II) reductase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0050787; P:detoxification of mercury ion; IEA:InterPro.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.30.70.100; -; 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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_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; PF00403; HMA; 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 SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000350};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000350};
KW Mercuric resistance {ECO:0000256|ARBA:ARBA00022466,
KW ECO:0000256|PIRNR:PIRNR000350};
KW Mercury {ECO:0000256|ARBA:ARBA00022914, ECO:0000256|PIRNR:PIRNR000350};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000350}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000350};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000350};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000183508}.
FT DOMAIN 6..69
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT BINDING 139
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 264..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 354
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 395
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 130..135
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 554 AA; 58865 MW; 2E8EE73CD1668C3B CRC64;
MQPEKQKVRL AVQGMTCTDC ERHVTLALQR VGAEGITASF RRGEATFEID PARLEEAKRA
VANSGYEPGA VEILDGSPRL GGPVQSGGGD HEYDLLIIGT GGAAFSAAIQ AVSYGAKVAM
VERGTIGGTC VNIGCVPSKT MLRASEINHL AAHNPFPGLH TSAGSVNLQQ LVGAKDELVA
ELRQHKYVDL IDEYGFHLIR GEARFVDPST VEVAGRNIRA RRYLIATGAS PALPDIAGLA
DVDYLVSTTA LDLTEIPRRL AVIGSGYIAL ELGQMFHRLG SEVTLMQRSD RLLKAYDQEV
SEAVAQVLSR EGIRSLTGVT YERVEQHGDV KRVHLTVNGQ EQVVEAEALL VATGRKPNTA
ALNLEAAQVR VGSRGEVLVD EYLRTSNPNV YAAGDVTLGP QFVYVAAYEG ALAAENAVGS
AQRKADLTVV PAVTFTSPAI ATVGMTEAKA RSKGYQVLTS VLPLEAVPRA LVNRDTAGLL
KLVADARTRK LLGVHVVAEN AGDVIYAGVL AVKFGLTIED LRSTLAPYLT MAEGLKLATL
TFDKDVSKLS CCAG
//
