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Database: UniProt
Entry: A0A1Q5JJD6_9ACTN
LinkDB: A0A1Q5JJD6_9ACTN
Original site: A0A1Q5JJD6_9ACTN 
ID   A0A1Q5JJD6_9ACTN        Unreviewed;       420 AA.
AC   A0A1Q5JJD6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:OKJ69427.1};
GN   ORFNames=AMK29_03095 {ECO:0000313|EMBL:OKJ69427.1};
OS   Streptomyces sp. CB02261.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703940 {ECO:0000313|EMBL:OKJ69427.1, ECO:0000313|Proteomes:UP000186742};
RN   [1] {ECO:0000313|EMBL:OKJ69427.1, ECO:0000313|Proteomes:UP000186742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02261 {ECO:0000313|EMBL:OKJ69427.1,
RC   ECO:0000313|Proteomes:UP000186742};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ69427.1}.
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DR   EMBL; LIVX01000001; OKJ69427.1; -; Genomic_DNA.
DR   RefSeq; WP_073807084.1; NZ_LIVX01000001.1.
DR   AlphaFoldDB; A0A1Q5JJD6; -.
DR   OrthoDB; 1145at2; -.
DR   Proteomes; UP000186742; 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; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
FT   DOMAIN          8..313
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          333..418
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   420 AA;  45064 MW;  336EB14AFDDD9236 CRC64;
     MVDADQTFVI VGGGLAGAKA AETLRSEGFN GRVILIGDER DHPYERPPLS KGYLTGAKER
     DSAFVHDAAW YAANDIELHL GQPVTAVDRE ARTVLLGDNT VIRYDKLLLA TGSEPRRLDV
     PGTELAGVHH LRRLAHADRL RQVLSGLGRD NGHLVIAGAG WIGLEVAAAA RGYGAEVTVV
     ESDPTPLHRV LGPELGQLFA DLHTDHGVRF HFGVRLTEIV GQDGMVLAVR TDDGEEHPAH
     AVLAAIGAAP RTALAENSGL ALVDRADGGG VAVDESLRTS DPDIYAAGDI AAAHHPLLHT
     RLRVEHWANA LNGGPAAARA MLGQPVSYDR VPYFFSDQYD LGMEYSGWAP PGTYDQVVVR
     GDTGKREFIA FWLKEGRVLA GMNVNVWDVT DPIQRIIRSK AAVHPDALAD PSVPLDSLIP
//
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