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Database: UniProt
Entry: A0A176LC71_9ACTN
LinkDB: A0A176LC71_9ACTN
Original site: A0A176LC71_9ACTN 
ID   A0A176LC71_9ACTN        Unreviewed;       421 AA.
AC   A0A176LC71;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:OAB02092.1};
GN   ORFNames=A6P39_03650 {ECO:0000313|EMBL:OAB02092.1};
OS   Streptomyces sp. FXJ1.172.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=710705 {ECO:0000313|EMBL:OAB02092.1};
RN   [1] {ECO:0000313|EMBL:OAB02092.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAB02092.1};
RA   Liu M., Liu N., Shang F., Huang Y.;
RT   "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT   from red soil-derived Streptomyces sp. FXJ1.172.";
RL   Submitted (APR-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:OAB02092.1}.
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DR   EMBL; LWRP01000019; OAB02092.1; -; Genomic_DNA.
DR   RefSeq; WP_067039364.1; NZ_CP119133.1.
DR   AlphaFoldDB; A0A176LC71; -.
DR   STRING; 710705.A6P39_03650; -.
DR   OrthoDB; 1145at2; -.
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.
PE   4: Predicted;
FT   DOMAIN          8..315
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          334..418
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   421 AA;  45570 MW;  C80F13A8CFE3A625 CRC64;
     MVDADQTFVI VGGGLAGAKA AETLRAEGFT GRVILISDER DHPYERPPLS KGYLLGKEER
     DSVFVHEPAW YAQNDIELHL GQFVDRIDRA AKTVRYGDDG TLVRYDKLLL VTGAEPRRLD
     IPGTGLAGVH HLRRLAHAER LKGVLAALGR DNGHLVIAGA GWIGLEVAAA AREYGAEVTV
     IDPEPTPLHH VLGPELGGVF AELHREHGVR FHFGRRLTEI VGQDGMVLAA RTDDGEEHPA
     HDVLAAIGAA PRTGLAEAAG LEIADRAHGG GIVVDERLRT SDPDIYAAGD VANFPLALFG
     TPLRVEHWAN ALNAGPAAAR SMLGQDVTYD RIPYFFTDQY DLGMEYSGWA PPGSYDQVVI
     RGDAGKREFI AFWLAEGRVL AGMNVNVWDV TEGIQKLIRS RQQVDPDALA DPHVPLDGLT
     S
//
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