MERA_SHIFL
ID MERA_SHIFL Reviewed; 564 AA.
AC P08332; P07045;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Mercuric reductase;
DE EC=1.16.1.1;
DE AltName: Full=Hg(II) reductase;
GN Name=merA;
OS Shigella flexneri.
OG Plasmid IncFII R100 (NR1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2989109; DOI=10.1016/0378-1119(85)90134-9;
RA Misra T.K., Brown N.L., Haberstroh L., Schmidt A., Goddette D., Silver S.;
RT "Mercuric reductase structural genes from plasmid R100 and transposon
RT Tn501: functional domains of the enzyme.";
RL Gene 34:253-262(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn21;
RX PubMed=6530603;
RA Barrineau P., Gilbert P., Jackson W.J., Jones C.S., Summers A.O.,
RA Wisdom S.;
RT "The DNA sequence of the mercury resistance operon of the IncFII plasmid
RT NR1.";
RL J. Mol. Appl. Genet. 2:601-619(1984).
RN [3]
RP SEQUENCE REVISION.
RA Summers A.O.;
RL Submitted (SEP-1986) 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 -!- 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; J01730; AAA92263.1; -; Genomic_DNA.
DR EMBL; K03089; AAB59078.1; -; Genomic_DNA.
DR PIR; A22799; RDEBHA.
DR AlphaFoldDB; P08332; -.
DR SMR; P08332; -.
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:0045454; P:cell redox homeostasis; IEA:InterPro.
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; 3.50.50.60; -; 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 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 SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR02053; MerA; 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; FAD; Flavoprotein; Mercuric resistance; Mercury;
KW Metal-binding; NADP; Oxidoreductase; Plasmid; Redox-active center;
KW Transposable element.
FT CHAIN 1..564
FT /note="Mercuric reductase"
FT /id="PRO_0000068001"
FT DOMAIN 1..65
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 11
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 14
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 127..135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 561
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT BINDING 562
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT DISULFID 135..140
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT VARIANT 70
FT /note="P -> A (in plasmid NR1)"
FT VARIANT 341..342
FT /note="VR -> EG (in plasmid NR1)"
SQ SEQUENCE 564 AA; 58975 MW; 582E74333BDA88EF CRC64;
MSTLKITGMT CDSCAVHVKD ALEKVPGVQS ADVSYAKGSA KLAIEVGTSP DALTAAVAGL
GYRATLADAP SVSTPGGLLD KMRDLLGRND KTGSSGALHI AVIGSGGAAM AAALKAVEQG
ARVTLIERGT IGGTCVNVGC VPSKIMIRAA HIAHLRRESP FDGGIAATTP TIQRTALLAQ
QQARVDELRH AKYEGILEGN PAITVLHGSA RFKDNRNLIV QLNDGGERVV AFDRCLIATG
ASPAVPPIPG LKDTPYWTST EALVSETIPK RLAVIGSSVV ALELAQAFAR LGAKVTILAR
STLFFREDPA IGEAVTAAFR MEGIEVREHT QASQVAYING VRDGEFVLTT AHGELRADKL
LVATGRAPNT RKLALDATGV TLTPQGAIVI DPGMRTSVEH IYAAGDCTDQ PQFVYVAAAA
GTRAAINMTG GDAALNLTAM PAVVFTDPQV ATVGYSEAEA HHDGIKTDSR TLTLDNVPRA
LANFDTRGFI KLVVEEGSGR LIGVQAVAPE AGELIQTAAL AIRNRMTVQE LADQLFPYLT
MVEGLKLAAQ TFNKDVKQLS CCAG
