ID   A0A345XUA0_9ACTN        Unreviewed;       471 AA.
AC   A0A345XUA0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Flavoprotein oxidoreductase {ECO:0000313|EMBL:AXK35216.1};
GN   ORFNames=DVA86_23830 {ECO:0000313|EMBL:AXK35216.1};
OS   Streptomyces armeniacus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=83291 {ECO:0000313|EMBL:AXK35216.1, ECO:0000313|Proteomes:UP000254425};
RN   [1] {ECO:0000313|EMBL:AXK35216.1, ECO:0000313|Proteomes:UP000254425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15676 {ECO:0000313|EMBL:AXK35216.1,
RC   ECO:0000313|Proteomes:UP000254425};
RA   Labana P., Gosse J.T., Boddy C.N.;
RT   "Draft genome of the type strain Streptomyces armeniacus ATCC 15676.";
RL   Submitted (JUL-2018) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP031320; AXK35216.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345XUA0; -.
DR   Proteomes; UP000254425; Chromosome.
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:UP000254425}.
FT   DOMAIN          2..310
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          349..451
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   471 AA;  49203 MW;  0FB103937CA15907 CRC64;
     MVIIGGDAAG MSAAAQARRL RTEDELEIVA FERGAFTSYS ACGIPYWIGG DVGSRDELIA
     RTPEEHRKRG IDVRLHTEVT AIDLDGQRVR TRAHGAAGGA AGGPRGAEEW TGFDKLVIAT
     GARPVRPSLP GMDADGVHGV QSLGDGEALL DSLAAAERAD GGARRTLRAV VVGAGYIGVE
     MSEALIRRGH RVTVLDRAEQ PMSTLDPDMG ALVREGMTGL GIDVRTGAAV TGIRTDADGR
     ARAVVTADGE HEADIVVLGI GVRPETALAE AAGLPLGDAG GLLTDLAMRV RGQRNVWAGG
     DCVEVFDRVT RRPRHLPLGT HANKHGQVIG TNAGGGYATF PGVVGTAVSK VCDLEIARTG
     LLERQAERAG LRFVTVTVEA TGRAGYFPGA EPMRVKMLAE RRTGRLLGTQ IVGREGAGKR
     VDIAAVALTA GMTVEEMTGL DLGYAPPFSP VWDPVLVAAR RAASEVRAQG S
//