ID   A0A1M3BBY6_9ACTN        Unreviewed;       410 AA.
AC   A0A1M3BBY6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=FAD-dependent oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BGO11_14980 {ECO:0000313|EMBL:OJU81466.1};
OS   Solirubrobacterales bacterium 70-9.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales.
OX   NCBI_TaxID=1895833 {ECO:0000313|EMBL:OJU81466.1, ECO:0000313|Proteomes:UP000184118};
RN   [1] {ECO:0000313|EMBL:OJU81466.1, ECO:0000313|Proteomes:UP000184118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-9 {ECO:0000313|EMBL:OJU81466.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:OJU81466.1}.
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DR   EMBL; MKSH01000217; OJU81466.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3BBY6; -.
DR   Proteomes; UP000184118; 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; IPR028202; Reductase_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
FT   DOMAIN          8..304
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          323..409
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   410 AA;  43419 MW;  961172381895A6B2 CRC64;
     MADREVDFLL VGGGLAGASC AAELRKRGAE GSILLVGREP EPPYERPPLS KEYLRGDASR
     ADAYVNEPAW YEENSVELMT GKNVMSIDAE AKTAKIQGGV EVAFGQALLG TGSNVNILRI
     EGAENEGIHY LRAYGNADAI REDAKAAERV VLVGGSYIAA EVAASLAATG THCTMVAVED
     VALSRTFGDD AGGFFQKGLE EHGVTFVGGE SVSAFEGDGR VSSVLTESGR SFDCDLVVVG
     AGVKPDVMIA QRAGLEVENG IVCDSKLQTS VPGIYAAGDV CSYDSVVHGR RIRVEHWDVA
     MQQGMHAAKN MLGAGEDYDV VPYFFSDLAD WASLEYVGPA ADWEQEVWRG SRDEGEFSVW
     YLKGGKVAGC LSVGRSEDLA EARRLLADGV DIGDAVDKIA DSDADLSSLG
//