ID A0A0F4JUJ4_9ACTN Unreviewed; 460 AA.
AC A0A0F4JUJ4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Flavoprotein oxidoreductase {ECO:0000313|EMBL:KJY38022.1};
GN ORFNames=VR44_04425 {ECO:0000313|EMBL:KJY38022.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY38022.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY38022.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY38022.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-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:KJY38022.1}.
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DR EMBL; JZWV01000081; KJY38022.1; -; Genomic_DNA.
DR RefSeq; WP_045946028.1; NZ_JZWV01000081.1.
DR AlphaFoldDB; A0A0F4JUJ4; -.
DR STRING; 68223.GCA_002028425_05448; -.
DR PATRIC; fig|68223.7.peg.454; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000033551; 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 5..304
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; 48228 MW; 7D96E91A89E55085 CRC64;
MAAERLVVVG GDAAGMSAAS QARRLKGAGE LEITAFERGH FTSYSACGIP YWVGGQVTER
DDLIARTPEE HRARGIDLRT RTEVLELDLP GRRVRARNLD SGEESWTGWD KLVLATGARP
VRPKLPGIGA HGVHGIQSLD DGQRLIGSLE RTEGRRAVVV GAGYIGVEMA EALVHRGYEV
TVLHRGPQPM ATLDPDMGGL VHRAMNAMGI VTVSGAEVVK ILEDEEGRAR AVATASGEEY
PADVVVLGIG VEPRTSLARE AGLPLGESGG LLTDLSMRVR GQEDVWAGGD CVEVLDLVAG
RNRHIPLGTH ANKHGQVIGS NVGGGYATFP GVVGTAVSKV CDLEIARTGL REKDALAAGL
RFVTATIRST NTAGYYPGAA EMTVKMLAER RTGRLLGVQI VGGAGSAKRV DVAAVALTAG
MTVEQVVALD LGYAPPFSPV WDPVLVAARK AVSAVRAAGV
//
