ID A0A0M8SQW5_9ACTN Unreviewed; 460 AA.
AC A0A0M8SQW5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Flavoprotein oxidoreductase {ECO:0000313|EMBL:KOU38542.1};
GN ORFNames=ADK55_34575 {ECO:0000313|EMBL:KOU38542.1};
OS Streptomyces sp. WM4235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415551 {ECO:0000313|EMBL:KOU38542.1, ECO:0000313|Proteomes:UP000037699};
RN [1] {ECO:0000313|EMBL:KOU38542.1, ECO:0000313|Proteomes:UP000037699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM4235 {ECO:0000313|EMBL:KOU38542.1,
RC ECO:0000313|Proteomes:UP000037699};
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:KOU38542.1}.
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DR EMBL; LGDE01000469; KOU38542.1; -; Genomic_DNA.
DR RefSeq; WP_053684726.1; NZ_LGDE01000469.1.
DR AlphaFoldDB; A0A0M8SQW5; -.
DR PATRIC; fig|1415551.3.peg.7538; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000037699; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000037699}.
FT DOMAIN 5..299
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 338..440
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 460 AA; 48381 MW; C3F2F56C0E231C38 CRC64;
MAAERLVVIG GDAAGMSAAS QARRLKGPAE LEITAFERGH FTSYSACGIP YWIGGQVAGR
DELIARTPEE HRARDIDLRI RNEVVELDLV GRRVRARDLD SGVESWTAYD KLVLATGARP
IRPRLPGIGA HGVHGVQSLD DGQRLMDGLE RTQGRRAVVV GAGYIGVEMA EALVGRGFEV
TVLHRGEQPM ATLDPDMGGL VHTAMNGMGI RTVSRAEVTR ILTDEDGRAC AVATAAGDEY
PADVVVLGMG VEPRTALARA AGLPLGDSGG LLTDLSMRVR GHEDIWAGGD CVEVLDLVAG
RPRHIPLGTH ANKHGQVIGS NVGGGYATFP GVVGTAVSKV CDLEIARTGL RERDAREAGL
RFVTATIRST NTAGYYPGAT EMTVKMLAER RTGRLLGVQI VGGAGAAKRV DIAAVALTAG
MTVDQVVSLD LGYAPPFSPV WDPILVAARK AVTAVRSAGV
//
