ID A0A254N183_9BURK Unreviewed; 560 AA.
AC A0A254N183;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:OWR00802.1};
GN ORFNames=CDO81_24030 {ECO:0000313|EMBL:OWR00802.1};
OS Roseateles puraquae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=431059 {ECO:0000313|EMBL:OWR00802.1, ECO:0000313|Proteomes:UP000197446};
RN [1] {ECO:0000313|EMBL:OWR00802.1, ECO:0000313|Proteomes:UP000197446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 52769 {ECO:0000313|EMBL:OWR00802.1,
RC ECO:0000313|Proteomes:UP000197446};
RX PubMed=17978231; DOI=10.1099/ijs.0.65149-0;
RA Gomila M., Bowien B., Falsen E., Moore E.R., Lalucat J.;
RT "Description of Pelomonas aquatica sp. nov. and Pelomonas puraquae sp.
RT nov., isolated from industrial and haemodialysis water.";
RL Int. J. Syst. Evol. Microbiol. 57:2629-2635(2007).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWR00802.1}.
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DR EMBL; NISI01000014; OWR00802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254N183; -.
DR OrthoDB; 178496at2; -.
DR Proteomes; UP000197446; 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; 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};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000197446}.
FT DOMAIN 1..65
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT BINDING 144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 276..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 361
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 402
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 135..140
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 560 AA; 58449 MW; 3B9707808609F65A CRC64;
MTELKINGMT CDACAVHVKQ ALESVPGVQS AEVSYAKGSA RLAIAGGTSP EALIAAVAGL
GYRAALADAS DPLPKGGRLD RARDWVAGGD KASHDGGLHI AVIGSGGAAM AAALKAVERG
ARVTLIERGT IGGTCVNVGC VPSKIMIRAA HIAHLRRESP FDGGLQANAP VVLRERLLVQ
QQARVDALRY AKYESILDGN PAITRLAGEA RFKDGHSLFV RLIEGREHVV SFDRCLIATG
AGAAVPPIPG LRDTPYWTST EALVSDTIPA RLAVIGSSVV AVELAQAFAR LGAKVTILAR
STLFSREDPA IGETVTAAFR AEGIEVLDHA QASQVAHMDG EFVLNTNQGE LRADRLLVAT
GRTPNTNSLN LEASGVTVDK QGAIEIDPGM RTSAPDIYAS GDCTDQPQFV YVAAAAGTRA
AINMTGGNAA LDLTAMPAVA FTDPQVATVG LSEQAAHDAG IETDSRTLTL DNVPRALANF
DTRGFIKLVI EEGSHRLIGV QAVAPEAGEL IQTAALAIRA RMTAQELAEQ LFPYLTMVEG
LKLAAQTFSK DVKQLSCCAG
//
