ID A0A0M8VHT2_9ACTN Unreviewed; 482 AA.
AC A0A0M8VHT2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Flavoprotein disulfide reductase {ECO:0000313|EMBL:KOV63637.1};
GN ORFNames=ADK64_18845 {ECO:0000313|EMBL:KOV63637.1};
OS Streptomyces sp. MMG1121.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV63637.1, ECO:0000313|Proteomes:UP000037687};
RN [1] {ECO:0000313|Proteomes:UP000037687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1121 {ECO:0000313|Proteomes:UP000037687};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-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:KOV63637.1}.
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DR EMBL; LGDV01000189; KOV63637.1; -; Genomic_DNA.
DR RefSeq; WP_053660403.1; NZ_LGDV01000189.1.
DR AlphaFoldDB; A0A0M8VHT2; -.
DR STRING; 1415544.ADK64_18845; -.
DR PATRIC; fig|1415544.3.peg.4063; -.
DR OrthoDB; 4678789at2; -.
DR Proteomes; UP000037687; 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: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:UP000037687}.
FT DOMAIN 6..341
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 362..468
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 126
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 198..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 482 AA; 50364 MW; 55EE9654E1909763 CRC64;
MGYVTRIVII GGGPGGYEAA LVAAQLGAEV TVVDCDGLGG ASVLTDCVPS KTLIATAEVM
TTFDSSYEEL GIIVADDTPP LEQAARVVGV DLGKVNRRVK RLALAQSHDI TASVTRAGAR
VLRGRGRLDG MQGLDGSRKV AVTAADGTEE ILTADAVLIA TGGHPRELPD AQPDGERILN
WTQVYDLTEL PQELIVVGSG VTGAEFAGAY QALGSKVTLV SSRDRVLPGE DPDAAAVLED
VFRRRGMNVM ARSRAQSAKR VGDRVEVMLA DGRVITGSHC LMAVGAIPNS AGLGLEEAGV
RLRDSGHIWT DKVSRTTAPG VYAAGDVTGV FALASVAAMQ GRIAMYHFLG DAVAPLNLKT
VSSNVFTDPE IATVGYTQAD VDAGKIDARV VKLPLLRNPR AKMQGIRDGF VKIFCRPGTG
IVVGGVVVAP RASELIHPIS IAVDNNLTVE QIANAFTVYP SLSGSIAEVA RQLHTRKASA
EA
//
