ID A0A176KYD0_9ACTN Unreviewed; 519 AA.
AC A0A176KYD0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Ferredoxin reductase {ECO:0000313|EMBL:OAA97285.1};
GN ORFNames=A6P39_29280 {ECO:0000313|EMBL:OAA97285.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA97285.1};
RN [1] {ECO:0000313|EMBL:OAA97285.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA97285.1};
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:OAA97285.1}.
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DR EMBL; LWRP01000156; OAA97285.1; -; Genomic_DNA.
DR RefSeq; WP_067052328.1; NZ_CP119133.1.
DR AlphaFoldDB; A0A176KYD0; -.
DR STRING; 710705.A6P39_29280; -.
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; 3.30.70.20; -; 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; PF13370; Fer4_13; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
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 86..389
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 413..484
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
FT REGION 485..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 53977 MW; 3A5150A76B83F35A CRC64;
MTVTVDLNRC QSYGQCTMMA PDVFRFSGEE SLEYDHVPPA AEDENVARAV AACPVQAITV
GQPSALAGVR RRGGPVAAGQ GGGPRRIVVV GASLAGLRAV EALRDEGFTG DITVIGDEPH
EPYDRPPLSK AVLTGRLDIE HVLMARPRDA GVRWLLGTAA GLDAPGRRVM LADGRVVPYD
RLLIATGVRA RELPGQDPAV RGVHRLRGRD DAERLRADLA AGPRRVLIVG GGLIGSEVAG
ACRSLGLPVT LVHRGPSPLS GALGTIVGGH AAGLQRDAGV DLRLESTVTA LETDGRGRLR
RARLSAGSGV DTDVAVISLG AVANVEWLRG AGLEAGPRGV VCDAKCRVLR SDGSADEEIF
AAGDVTRWPH PLYDGRLISL GHWGNAVAQA QAAAHNMTCA PSNRRDYAPL PAFWSDQFGA
NIKVVGVPSL ADSTVLTQGS LADGRFVVAY GLHGRLVAAA AVNSPRVLDG YAALIRARAP
FPPRINAGDS PPELIPQDAG FSGAAGGAPR PLVPSSPLQ
//
