ID A0A0M8XYU3_9ACTN Unreviewed; 457 AA.
AC A0A0M8XYU3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Flavoprotein oxidoreductase {ECO:0000313|EMBL:KOX15862.1};
GN ORFNames=ADL06_34340 {ECO:0000313|EMBL:KOX15862.1};
OS Streptomyces sp. NRRL F-6491.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX15862.1, ECO:0000313|Proteomes:UP000037743};
RN [1] {ECO:0000313|EMBL:KOX15862.1, ECO:0000313|Proteomes:UP000037743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX15862.1,
RC ECO:0000313|Proteomes:UP000037743};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:KOX15862.1}.
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DR EMBL; LGEE01000283; KOX15862.1; -; Genomic_DNA.
DR RefSeq; WP_053642002.1; NZ_LGEE01000283.1.
DR AlphaFoldDB; A0A0M8XYU3; -.
DR PATRIC; fig|1519495.3.peg.7328; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000037743; 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; 3.50.50.60; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 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; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 4..311
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 336..438
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 457 AA; 48241 MW; CAF059D3871A2057 CRC64;
MSERLVVIGG DAAGMSAASQ ARRLRSPGEL EIVAFERGHF SSYSACGIPY WVGGDVGSRD
ELIARSPEEH RARDIGLRTR TEVTEIDVER QRVRSRDLES GTEEWTGFDK LVIATGARPL
RPPVPGIDAP GVHGVQNLED GQALIDALSG AEGRRAVVVG AGYIGVEMAE ALLNRGYEVT
VLNRSERPMA TLDPDMGRLV HEAMDGLGIR TVNSAAVTKV LTGPDGRVRA VATDEEEYPA
DVVVLGTGVE PETSLAREAG LPLGAYGGLL TDLGMRVRGH ENVWAGGDCV EVLDLVSGRT
RHVALGTHAN KQGQVIGSNV GGDYATFPGM VGTAVSKVCD LEIARTGLRE KEALEAGLRF
VTVTVESTSR AGYYPGAAPM TVKMLAERRT GRLLGTQIVG REGAAKRVDV AAVALTAKMT
VEAMTALDLG YAPPFSPVWD PVLVAARKAT AAVRAAG
//
