ID G9AI44_RHIFH Unreviewed; 745 AA.
AC G9AI44;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 Name=merA2 {ECO:0000313|EMBL:CCF00726.1};
GN OrderedLocusNames=SFHH103_06267 {ECO:0000313|EMBL:CCF00726.1};
OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OG Plasmid pSfHH103e {ECO:0000313|EMBL:CCF00726.1,
OG ECO:0000313|Proteomes:UP000007735}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCF00726.1, ECO:0000313|Proteomes:UP000007735};
RN [1] {ECO:0000313|EMBL:CCF00726.1, ECO:0000313|Proteomes:UP000007735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH103 {ECO:0000313|EMBL:CCF00726.1,
RC ECO:0000313|Proteomes:UP000007735};
RC PLASMID=pSfHH103e {ECO:0000313|Proteomes:UP000007735};
RX PubMed=22374952; DOI=10.1128/JB.06729-11;
RA Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA Vinardell J.M., Zehner S., Gottfert M.;
RT "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL J. Bacteriol. 194:1617-1618(2012).
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; HE616899; CCF00726.1; -; Genomic_DNA.
DR RefSeq; WP_014332372.1; NC_016815.1.
DR AlphaFoldDB; G9AI44; -.
DR KEGG; sfh:SFHH103_06267; -.
DR PATRIC; fig|380.5.peg.5821; -.
DR HOGENOM; CLU_020731_0_0_5; -.
DR Proteomes; UP000007735; Plasmid pSfHH103e.
DR GO; GO:0018836; F:alkylmercury lyase activity; IEA:InterPro.
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 GO; GO:0046413; P:organomercury catabolic process; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.30.450.410; -; 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; IPR004927; MerB.
DR InterPro; IPR021179; Mercury_reductase_MerA.
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; PF03243; MerB; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 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 SUPFAM; SSF160387; NosL/MerB-like; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691}; Plasmid {ECO:0000313|EMBL:CCF00726.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691}.
FT DOMAIN 284..597
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 621..729
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 77946 MW; 7465C965082A53C1 CRC64;
MNNCCASSPS PGKAGISTPA TPPSFAVRPG VTFPDWSVVR LPAVRDALQA MVGSDHVLNR
WSGYDPATDR VRVALLKLYA EDGRAPSRSA LAERAELSET AILPLLEELR RRDLVVLDER
IVGAYPFTDR HTGHRVTLDG HVLNAMCAVD ALGIGAMTDR DIAITSQCRH CDAPIRITSR
RRGRILAAVE PSTAVMWQSV RYEGGCAASS LCATTAFFCS DEHLSAWRDE RSADESGFRL
SIEEGLQAGR ALFGPSLAGL DVGSKSTAVA SRPFPAHGRN GGGYDLVVIG AGSAGFSAAI
TAADQGAQVG LIGSGTIGGT CVNVGCVPSK TLIRAAETLH NARVAARFAG IAAEAELTDW
RGTIRQKDAL VSELRQAKYV DLLPAYNGIA YRDGPARLID GGVEVNGTRI PAGKIVIATG
ARPAVPIIPG IETVPYLTST TALELEKLPS SLLVIGGGYI GAELAQMFSR AGVKVMLVCR
SRLLPEAEPE IGAALTGYFE DEGITVVSGI AYRAIRKTEG GVLLTVTRDG EDVAIDADQV
LISTGRTPNI EGLGLAEYGI AVSPKGGIVV DDRMRTTKAG VYAAGDVTGR DQFVYMAAYG
AKLAANNALN GDGLCYDNGT MPAIVFTDPQ VASVGLTEAA ARAEGHEVRV STIGLDQVPR
ALAARDTRGL IKLVADANSA RLLGAHILAP EGADSIQTAT LAIRQGLTVD DLADMIFPYL
TTVEGLKLAA LAFGKDVAKL SCCAG
//
