ID F4B6G8_ACIHW Unreviewed; 435 AA.
AC F4B6G8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Mercuric reductase {ECO:0000256|ARBA:ARBA00014791};
DE EC=1.16.1.1 {ECO:0000256|ARBA:ARBA00012661};
DE AltName: Full=Hg(II) reductase {ECO:0000256|ARBA:ARBA00031725};
GN OrderedLocusNames=Ahos_1711 {ECO:0000313|EMBL:AEE94588.1};
OS Acidianus hospitalis (strain W1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=933801 {ECO:0000313|EMBL:AEE94588.1, ECO:0000313|Proteomes:UP000008458};
RN [1] {ECO:0000313|EMBL:AEE94588.1, ECO:0000313|Proteomes:UP000008458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1 {ECO:0000313|EMBL:AEE94588.1,
RC ECO:0000313|Proteomes:UP000008458};
RX PubMed=21607549; DOI=10.1007/s00792-011-0379-y;
RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA She Q., Liu S.J., Garrett R.A.;
RT "Genomic analysis of Acidianus hospitalis W1 a host for studying
RT crenarchaeal virus and plasmid life cycles.";
RL Extremophiles 15:487-497(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W1;
RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA Liu S.J., Garrett R.A.;
RT "Genomic analyses of Acidianus hospitalis W1 a host for studying
RT crenarchaeal virus and plasmid life cycles.";
RL Extremophiles 0:0-0(2011).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; CP002535; AEE94588.1; -; Genomic_DNA.
DR RefSeq; WP_013776503.1; NC_015518.1.
DR AlphaFoldDB; F4B6G8; -.
DR STRING; 933801.Ahos_1711; -.
DR GeneID; 10601211; -.
DR KEGG; aho:Ahos_1711; -.
DR eggNOG; arCOG01068; Archaea.
DR HOGENOM; CLU_016755_1_1_2; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000008458; Chromosome.
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:0050787; P:detoxification of mercury ion; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 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; 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; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691}.
FT DOMAIN 2..285
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 317..418
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 435 AA; 47741 MW; 3E679254D84F3517 CRC64;
MKDLVIIGYG AAGFASLIEA NELGIKPVLI GYGPIGGTCV NVGCVPSKRL LHLGEKGRDF
FSSFEDTKQF VNRSRKEKYE DVLSYYDVEL IEGKAHFISP HEVKVGDKVI EGKKFIIATG
SSPFIPEIPG LKDLGYWTNV EALNPDRKIS SLVIIGGRAE ALEFSQMYRN FGVEVAILQR
SKTLIPDWEP EISLEIQKVL EEKGIYVVTD VKVKEVKKGE GGKVVVTNKG EVEAEEILMA
TGRKPNVDLN LSSAGVELNE KGGIKVNDEL QTTNPNIYAA GDVIGDKMLE ALAGYEGTVA
VRNAIKGEHK KIDFLSVPQV IFTRPNLARV GLNSFDGDFD SRTVKMKDIV KAQIIDEEKG
LIKMVVEKGS KRIMGVHVMA ENAAEFIGEA ALAIKHRMTI DDIIDTVHVF PTVAESLRIV
ALAFYKDVKK LSCCV
//
