MERA_ACIFR
ID MERA_ACIFR Reviewed; 547 AA.
AC P17239;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Mercuric reductase;
DE EC=1.16.1.1;
DE AltName: Full=Hg(II) reductase;
GN Name=merA;
OS Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=920;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RC STRAIN=E-15;
RX PubMed=2691338; DOI=10.1016/0378-1119(89)90138-8;
RA Inoue C., Sugawara K., Shiratori T., Kusano T., Kitagawa Y.;
RT "Nucleotide sequence of the Thiobacillus ferrooxidans chromosomal gene
RT encoding mercuric reductase.";
RL Gene 84:47-54(1989).
RN [2]
RP SEQUENCE REVISION TO 92; 440; 454-455 AND 483.
RA Inoue C., Sugawara K., Shiratori T., Kusano T., Kitagawa Y.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC STRAIN=E-15;
RX PubMed=2265748; DOI=10.1016/0378-1119(90)90349-v;
RA Inoue C., Sugawara K., Kusano T.;
RT "Thiobacillus ferrooxidans mer operon: sequence analysis of the promoter
RT and adjacent genes.";
RL Gene 96:115-120(1990).
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; D90110; BAA14139.3; -; Genomic_DNA.
DR PIR; JQ0153; JQ0153.
DR RefSeq; WP_012537218.1; NZ_JABFOH010000009.1.
DR AlphaFoldDB; P17239; -.
DR SMR; P17239; -.
DR STRING; 380394.Lferr_2107; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Mercuric resistance; Mercury; Metal-binding; NADP; Oxidoreductase;
KW Redox-active center.
FT CHAIN 1..547
FT /note="Mercuric reductase"
FT /id="PRO_0000068005"
FT DOMAIN 5..70
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 16
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 19
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 114..122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT BINDING 545
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT DISULFID 122..127
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 547 AA; 57438 MW; C33F3168CF62DEF5 CRC64;
MTENAPTELA ITGMTCDGCA AHVRKALEGV PGVREAQVSY PDATARVVLE GEVPMQRLIK
AVVASGYGVH PRSDGASSTN DGQELHIAVI GSGGAAMACA LKAVERGARV TLIERSTIGG
TCVNIGCVPS KIMIRAAHIA HLRRESPFDG GIQAVAPTIQ RTALLVQQQA RVDELRHAKY
EGILDGNPAI TVLRGEARFK DSRSVVVHLN DGGERVVMFD RCLVATGASP AVPPIPGLKD
TPYWTSTEGL VSESIPERLA VIGSSVVALE LAQAFARLGS HVTILARGTL FLREDPAIGE
AITAAFRAEG IEVLEHTQAS QVAYADGEFV LATGHGELRA DKLLVATGRA PNTRRLNLEA
AGVAINAQGA IVIDQGMRTN SPNIYAAGDC TDQPQFVYVA AAAGTRAAIN MMGGSAALDL
TAMPAVVFTD PQVATVGYSG AEAHRDGIET DSRTLTLDNV PRALANFNTR GFIKLVAEVG
SGRLIGVQVV APEAGELIQT AALAIRNRMT VQELADQLFP YLTMVEGLKL AAQTFTRDVK
QLSCCAG
