ID T0J2Q6_9SPHN Unreviewed; 492 AA.
AC T0J2Q6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Mercuric reductase {ECO:0000313|EMBL:EQB31092.1};
DE EC=1.16.1.1 {ECO:0000313|EMBL:EQB31092.1};
GN ORFNames=M529_16215 {ECO:0000313|EMBL:EQB31092.1};
OS Sphingobium ummariense RL-3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1346791 {ECO:0000313|EMBL:EQB31092.1, ECO:0000313|Proteomes:UP000015523};
RN [1] {ECO:0000313|EMBL:EQB31092.1, ECO:0000313|Proteomes:UP000015523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL-3 {ECO:0000313|EMBL:EQB31092.1,
RC ECO:0000313|Proteomes:UP000015523};
RX PubMed=24233594;
RA Kohli P., Dua A., Sangwan N., Oldach P., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium ummariense Strain RL-3, a
RT Hexachlorocyclohexane-Degrading Bacterium.";
RL Genome Announc. 1:e00956-13(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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:EQB31092.1}.
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DR EMBL; AUWY01000111; EQB31092.1; -; Genomic_DNA.
DR AlphaFoldDB; T0J2Q6; -.
DR STRING; 1346791.M529_16215; -.
DR PATRIC; fig|1346791.3.peg.3124; -.
DR eggNOG; COG1249; Bacteria.
DR Proteomes; UP000015523; Unassembled WGS sequence.
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:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 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|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000015523}.
FT DOMAIN 40..353
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 378..482
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 473
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 209..216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 76..81
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 492 AA; 52040 MW; F2A9F6CB6D905443 CRC64;
MLCSFALSRS CPSMAASHRE RFDELPNTSR DARAMSQTFD AIIIGAGQAG PPLAGRLTAA
GWKVALVERK LIGGTCVNTG CMPTKALVAS AYAAHLARRQ DLGVIVGDVR VDMKAVAARA
RKVADDARER NEQWLGKMKG LTLLRGHARL TGPSQVEVDG VALTAPHIFL NVGGRASVPD
MPGVGDVPHL DNTDMVALDS LPDHLVVVGG SYIGLEFAQM YARFGAKVTI VERGERLIAR
EDPEISDAIR AFVEAEGITV RTDADCIGFK PHPSGVIVTV ACRNGEPEVV GSHVLLAVGR
RPNTDDLGLD AAGVATDERG YIKVDDRLAT SVPGIWALGD CNGRGAFTHT AYNDFEIVAA
NLLDGADRRL GQRIPGYALY TDPPLGRAGM TETEARAKGH DVLVSSRPMS RVGRAVEKGE
TLGLMKVVAD RATRHILGAA ILGTSGDEAI HGILDAMSAG EPVDTLRWAV PVHPTVSELI
PTLLLGLDQG SA
//
