ID A0A1L3MIE7_9MICO Unreviewed; 471 AA.
AC A0A1L3MIE7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Flavoprotein disulfide reductase {ECO:0000313|EMBL:APH02068.1};
GN ORFNames=ASJ30_11475 {ECO:0000313|EMBL:APH02068.1};
OS Janibacter indicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=857417 {ECO:0000313|EMBL:APH02068.1, ECO:0000313|Proteomes:UP000182938};
RN [1] {ECO:0000313|EMBL:APH02068.1, ECO:0000313|Proteomes:UP000182938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YFY001 {ECO:0000313|EMBL:APH02068.1,
RC ECO:0000313|Proteomes:UP000182938};
RA Zhang Y., Guo Z.;
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}.
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DR EMBL; CP013290; APH02068.1; -; Genomic_DNA.
DR RefSeq; WP_072625224.1; NZ_CP013290.1.
DR AlphaFoldDB; A0A1L3MIE7; -.
DR KEGG; jte:ASJ30_11475; -.
DR Proteomes; UP000182938; Chromosome.
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:SF1; NAD(P)H DEHYDROGENASE (QUINONE); 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:UP000182938}.
FT DOMAIN 9..334
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 356..461
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 191..198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 471 AA; 48500 MW; 8500BF76DFEA1C2B CRC64;
MGDVTRTSSV VILGGGPGGY EAALVAAHLG ASVTVVDRDG IGGAAVLTDC VPSKTLIATA
DYLGGIETAS ELGVHLEDHE GDVATETVAE LDAINRRVLS LAAAQSADIT ARLQEVGVRV
VSGTGRLASP SEVVVEGTDG AIETISADVV LLSTGATPRV LPSAQPDGER ILTWQQVYEL
PEIPDKLIVV GSGVTGAELA QAYLGLGTDV TLISSRDLVL PGEDQDAAAV IEDVFRRRGM
TVLNRSRMAS AERRGDGVVV TLEDGREVEG SHVLIAVGAV PNTRDIGLEE VGVELSESGH
IVTDRVSRTS VRGVYAAGDC TGVFALASVA AMQGRTAMAH ALGDAVTPLR LSAVSANVFT
DPEIATVGMS AADAADNSDV EAVMMPLSRN PRAKMLGIAE GFVKLFAYRG TGTLLGGVVV
APRASELIFP VALAVANRLS VDQVASTFTV YPSLTGTIAE AARRLHPLHG E
//
