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Database: UniProt
Entry: A0A160NY18_STRLU
LinkDB: A0A160NY18_STRLU
Original site: A0A160NY18_STRLU 
ID   A0A160NY18_STRLU        Unreviewed;       420 AA.
AC   A0A160NY18;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Ferredoxin reductase {ECO:0000313|EMBL:BAU83016.1};
GN   ORFNames=SLA_2082 {ECO:0000313|EMBL:BAU83016.1};
OS   Streptomyces laurentii.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=39478 {ECO:0000313|EMBL:BAU83016.1, ECO:0000313|Proteomes:UP000217676};
RN   [1] {ECO:0000313|EMBL:BAU83016.1, ECO:0000313|Proteomes:UP000217676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31255 {ECO:0000313|EMBL:BAU83016.1,
RC   ECO:0000313|Proteomes:UP000217676};
RA   Doi K., Fujino Y., Nagayoshi Y., Ohshima T., Ogata S.;
RT   "Complete Genome Sequence of Thiostrepton-Producing Streptomyces laurentii
RT   ATCC 31255.";
RL   Genome Announc. 4:e00360-16(2016).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; AP017424; BAU83016.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A160NY18; -.
DR   KEGG; slau:SLA_2082; -.
DR   Proteomes; UP000217676; 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:UP000217676}.
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;  45133 MW;  6558C9E9E02BFD81 CRC64;
     MVDADQTFVI VGGGLAGAKA AETLRSEGFN GRVILVCDEH ERPYERPPLS KGFLLGKADR
     DSVFVHEPSW YASNDVELHL GQTVTAIDRD AHTVRLGDGT VIRYDKLLLA TGAEPRRLDI
     PGTGLAGVHH LRRLAHCERL RDELKALGRD NGHLVIAGAG WIGLEVAAAA RTYGAEVTIV
     EADPTPLHRV LGPELGQVFA DLHAAHGVRF HFGARLTEIT GQDGMVLAAR TDDGEEHPAH
     AVLVAIGAAP RTTLAENAGL ALVDRADGGG VAVDETLRTS DPDVFAAGDV AAAHHPALHT
     RLRVEHWANA LNGGPAAARA MLGQSVSYDR VPYFFSDQYD LGMEYSGWAP PGSYDQIVTR
     GDVGKREFVA FWLKDGRVLA GMNVNVWDVT EPIQKLIRSR AQVDPERLAD PSVPLETLAA
//
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