ID A0A0Q6Q688_9MICO Unreviewed; 463 AA.
AC A0A0Q6Q688;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Mercuric reductase {ECO:0000313|EMBL:KQV08137.1};
GN ORFNames=ASC63_13435 {ECO:0000313|EMBL:KQV08137.1};
OS Leifsonia sp. Root112D2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV08137.1, ECO:0000313|Proteomes:UP000051914};
RN [1] {ECO:0000313|EMBL:KQV08137.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV08137.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV08137.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV08137.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KQV08137.1}.
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DR EMBL; LMCU01000001; KQV08137.1; -; Genomic_DNA.
DR RefSeq; WP_055814307.1; NZ_LMCU01000001.1.
DR AlphaFoldDB; A0A0Q6Q688; -.
DR STRING; 1736426.ASC63_13435; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000051914; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000051914}.
FT DOMAIN 7..323
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 345..453
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 443
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 182..189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 44..49
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 463 AA; 48441 MW; 830567EA42D9295F CRC64;
MEAIEEFDLV VVGGGKGGKS LAMDRAKAGA RVAMVERGMI GGSCINVACI PTKTLVTSAR
AVGTIARAAK LGIRVDGSHV DLDLLRAHKE GVVGDMVKMN YDLFIASGMD FILGSARFTA
PRTIEVTTDA GRTRLLRGTE VVINTGTRPI VPAIEGIDTV GVMTSEDVLR LESIPGRVAV
IGGGYIGAEL AQMLHRFGSE LTMLVRGERL LAREEPEISQ ALAEVFTAEG IDVRFGAEAT
QVARQDDGAI EITLGDTSRL TVDALVVATG REPVTEGLHL HEAGVETNAA GFVIVDEKLA
TTAAHTWAAG DVAGHPQFTH VSFDDFRILK ANITGGDRST SGRLIPSVVF VEPEIATIGL
TEADARAAGI DVVVAAQPVI AVPRSRTLRQ TKGLWKIVID RASDRIVGAS LMGAESGEVL
AVIQVAMLAG APFTLLRDAI LAHPTMAEGL NTAFAGVTAS SAP
//
