ID A0A1D8T9S6_9NOCA Unreviewed; 383 AA.
AC A0A1D8T9S6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AOW94356.1};
GN ORFNames=BFN03_03140 {ECO:0000313|EMBL:AOW94356.1};
OS Rhodococcus sp. WMMA185.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW94356.1, ECO:0000313|Proteomes:UP000178767};
RN [1] {ECO:0000313|EMBL:AOW94356.1, ECO:0000313|Proteomes:UP000178767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMA185 {ECO:0000313|EMBL:AOW94356.1,
RC ECO:0000313|Proteomes:UP000178767};
RA Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT "Draft Genome of Rhodococcus sp. WMMA185.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; CP017014; AOW94356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D8T9S6; -.
DR STRING; 679318.BFN03_03140; -.
DR KEGG; rhw:BFN03_03140; -.
DR Proteomes; UP000178767; Chromosome.
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; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000178767}.
FT DOMAIN 1..286
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 307..374
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 383 AA; 40601 MW; 19C3821E8861BA43 CRC64;
MAGLRTAEEL RRAGYDGELV LVGGEPHLPY DRPPLSKEVL RGERSETTLK PREFFDEKNI
ELRLGVEAVS VDAERRVVCL ADRTQLDYDE LVVATGLVPR RIPGLQDLAG VHVLRSIDES
LALRGDLAEG KRALIVGAGF IGCELAASMR AGGLDVVLVE PQPAPLASVL GEEIGGLVAR
LHRAEGVELR SGVGLTSLRG TDRVTGAVLG DGSEVQVDVV AIGVGSLPVT EWLEGSGVEL
DNGVVCDGVG RTTVPHIWAV GDVAAWQLQV GDRRRVEHWS NAGEQAKILA GALTGTGDDN
RVAQVPYFWS DQYDIKIQAL GTVAPTDEVH VIKDDGRKFL AYYEREGKLV GVVGGGMAGG
VMKMRGKIAA GTPIGEVLEA ASA
//
