ID   A0A260X056_9NOCA        Unreviewed;       385 AA.
AC   A0A260X056;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OZF54458.1};
GN   ORFNames=CH292_06590 {ECO:0000313|EMBL:OZF54458.1};
OS   Rhodococcus sp. 14-2470-1a.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=2023150 {ECO:0000313|EMBL:OZF54458.1, ECO:0000313|Proteomes:UP000215821};
RN   [1] {ECO:0000313|Proteomes:UP000215821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14-2470-1a {ECO:0000313|Proteomes:UP000215821};
RA   Savory E.A., Fuller S.J., Weisberg A.J., Thomas W.J., Gordon M.I.,
RA   Stevens D.M., Creason A.L., Belcher M.S., Wiseman M., Putnam M.L.,
RA   Grunwald N.J., Chang J.H.;
RT   "Evolutionary transitions between beneficial and phytopathogenic
RT   Rhodococcus challenge disease management.";
RL   Submitted (JUL-2017) 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:OZF54458.1}.
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DR   EMBL; NPFZ01000014; OZF54458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A260X056; -.
DR   Proteomes; UP000215821; 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; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
FT   DOMAIN          2..268
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          304..384
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   385 AA;  40687 MW;  F89FFC260EB748D3 CRC64;
     MMRVVIVGGG LAGARSCETL RARGFEGEIV LLAAEKHLPY DRPPLTKAAL KGELNTQLRT
     DYDALSIDVR TATAATGLDT SARKVHTAGG PVEYDALIIA TGAAPIRLPG TDRQLAVRTV
     DDSYALREKL VPGTKVVLVG ASWIGAEVAT AALAAGAEVT CIEFGPAPLG NALGEEVGKR
     FVDWWSEVDL RLGVGVREVT DTGVSLTTGE EIPADVVVAG VGVRPDVAWL EGSGLEIERG
     IVVDENLRTS DPHVFAVGDV AVRWSPRSSQ PLLVEHWDDA RTGPDSIAQT LTGGEPVAHD
     PVPYFWSDQF GHKLQYVGHH AATDTVVVRD GVDGKWAVAW IDEAGLLTAH LSIDTPKLMI
     GARAAIAACS RPDAAALRDI TQPLS
//