ID Q56447_9XANT Unreviewed; 548 AA.
AC Q56447;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 133.
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 ECO:0000313|EMBL:AAA98326.1};
OS Xanthomonas sp. W17.
OG Plasmid RP1 {ECO:0000313|EMBL:AAA98326.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=138071 {ECO:0000313|EMBL:AAA98326.1};
RN [1] {ECO:0000313|EMBL:AAA98326.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W17 {ECO:0000313|EMBL:AAA98326.1};
RC PLASMID=RP1 {ECO:0000313|EMBL:AAA98326.1};
RX PubMed=8387603; DOI=10.1006/jmbi.1993.1228;
RA Kholodii G.Ya., Yurieva O.V., Lomovskaya O.L., Gorlenko Zh.M.,
RA Mindlin S.Z., Nikiforov V.G.;
RT "Tn5053, a mercury resistance transposon with integron's ends.";
RL J. Mol. Biol. 230:1103-1107(1993).
RN [2] {ECO:0000313|EMBL:AAA98326.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W17 {ECO:0000313|EMBL:AAA98326.1};
RC PLASMID=RP1 {ECO:0000313|EMBL:AAA98326.1};
RX PubMed=8594337; DOI=10.1111/j.1365-2958.1995.mmi_17061189.x;
RA Kholodii G.Y., Mindlin S.Z., Bass I.A., Yurieva O.V., Minakhina S.V.,
RA Nikiforov V.G.;
RT "Four genes, two ends, and a res region are involved in transposition of
RT Tn5053: a paradigm for a novel family of transposons carrying either a mer
RT operon or an integron.";
RL Mol. Microbiol. 17:1189-1200(1995).
RN [3] {ECO:0000313|EMBL:AAA98326.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W17 {ECO:0000313|EMBL:AAA98326.1};
RC PLASMID=RP1 {ECO:0000313|EMBL:AAA98326.1};
RA Kholodii G.Y.;
RT "Inversion activity of the Tn5053 and Tn402 resolution system, which
RT possess an uncommon res region.";
RL Russ. J. Genet. 31:1447-1451(1995).
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; L40585; AAA98326.1; -; Genomic_DNA.
DR AlphaFoldDB; Q56447; -.
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; PR00945; HGRDTASE.
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}; Plasmid {ECO:0000313|EMBL:AAA98326.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 1..65
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT BINDING 132
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 349
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 390
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 123..128
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 548 AA; 57483 MW; 1EC0AF82E8386603 CRC64;
MTEITVNGMT CTSCATHVKD ALEKIPGVNA AVVSYPESRA QVMADTAVSH NQLLAAIAAL
GYQGSIRVGD FKDEPKIRDA LEGAGLHIAI IGSGGAAMAA ALKAVEQGAT VTLIERGTIG
GTCVNIGCVP SKIMIRAAHI AHLRRESPFD GGIAATVPAI DRSKLLAQQQ ARVDELRHAK
YEGILDGNPA ITVLHGEARF KDDQSLVVRL NEGGEREVTF DRCLVATGAS PVVPPIPGLK
ESPYWTSTEA LVSDTIPARL AVIGSSVVAL ELAQAFARLG SQVTILARST LFFREDPAIG
EAVTAAFRAE GIEVLEHTQA SQVAHVNGEF VLTTGHGELR ADKLLVATGR APNTRSLALD
AAGVTVNAQG AIVIDQGMRT SNPNIYAAGD CTDQPQFVYV AAAAGTRAAI NMTGGDAALN
LTAMPAVVFT DPQVATVGYS EAEAHHDGIE TDSRTLTLDN VPRALANFDT RGFIKLVIEE
GSGRLIGVQA VAPEAGELIQ TAVLAIRNRM TVQELADQLF PYLTMVEGLK LAAQTFNKDV
KQLSCCAG
//
