ID F4GN28_PUSST Unreviewed; 561 AA.
AC F4GN28;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 OrderedLocusNames=PT7_0583 {ECO:0000313|EMBL:AEC19123.1};
OS Pusillimonas sp. (strain T7-7).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pusillimonas.
OX NCBI_TaxID=1007105 {ECO:0000313|EMBL:AEC19123.1, ECO:0000313|Proteomes:UP000008737};
RN [1] {ECO:0000313|EMBL:AEC19123.1, ECO:0000313|Proteomes:UP000008737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T7-7 {ECO:0000313|EMBL:AEC19123.1,
RC ECO:0000313|Proteomes:UP000008737};
RX PubMed=21622753; DOI=10.1128/JB.05242-11;
RA Cao B., Ma T., Ren Y., Ren Y., Li G., Li P., Guo X., Ding P., Feng L.;
RT "Complete genome sequence of Pusillimonas sp. T7-7, a cold-tolerant diesel
RT oil-degrading bacterium isolated from the Bohai Sea in China.";
RL J. Bacteriol. 193:4021-4022(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T7-7;
RA Cao B., Ma T., Li P., Jiang L., Li Y., Guo X., Feng L.;
RT "Genome Announcement Complete Genome Sequence of Pusillimonas sp. T7-7, a
RT novel species isolated from the Bohai Sea, China.";
RL Submitted (APR-2011) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002663; AEC19123.1; -; Genomic_DNA.
DR RefSeq; WP_005798829.1; NC_015458.1.
DR AlphaFoldDB; F4GN28; -.
DR STRING; 1007105.PT7_0583; -.
DR GeneID; 84796418; -.
DR KEGG; put:PT7_0583; -.
DR PATRIC; fig|266265.5.peg.8963; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_1_4; -.
DR OrthoDB; 178496at2; -.
DR Proteomes; UP000008737; Chromosome.
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}.
FT DOMAIN 1..65
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT BINDING 145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 277..284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 362
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 403
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 136..141
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 561 AA; 58635 MW; B908167705E75770 CRC64;
MTTLKITGMT CDSCAAHVKE ALEKVPGVQS ALVSYPKGTA QLAIEAGTSS DALTTAVAGL
GYEATLADAP PTDNRAGLLD KMRGWIGAAD KPSGNERPLQ VVVIGSGGAA MAAALKAVEQ
GAHVSLIERG TIGGTCVNVG CVPSKIMIRA AHIAHLRRES PFDGGIAATV PAIDRSKLLA
QQQARVEELR HAKYEGILDG NPAITVVHGE ARFKDEQSLV VRLNDGGERV VAFDRCLVAT
GASPAVPPIP GLKESPYWTS TEALVSDTLP ERLAVIGSSV VALELAQAFA RLGSQVTILA
RNTLFFRDDP SIGEAVTAAF RAEGIKVLEH TQASQVAHVN GEFVLTTGHG EVRADKLLVA
TGRTPNTRSL ALDAAGVTVN AQGAIVIDKG MRTSTPHIYA AGDCTDQPQF VYVAAAAGTR
AAINMTGGDA AINLTAMPAV VFTDPQVATV GYSEAEAHHD GIETDSRTLT LDNVPRALAN
FDTRGFIKLV IEEGSGRLIG VQVVAPEAGE LIQTAVLAIR NRMTVQELAD QLFPYLTMVE
GLKLAAQTFS KDVKQLSCCA G
//
