ID A0A1Q5L3P5_9ACTN Unreviewed; 463 AA.
AC A0A1Q5L3P5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ferredoxin reductase {ECO:0000313|EMBL:OKJ88450.1};
GN ORFNames=AMK31_08130 {ECO:0000313|EMBL:OKJ88450.1};
OS Streptomyces sp. TSRI0107.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ88450.1, ECO:0000313|Proteomes:UP000185813};
RN [1] {ECO:0000313|EMBL:OKJ88450.1, ECO:0000313|Proteomes:UP000185813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ88450.1,
RC ECO:0000313|Proteomes:UP000185813};
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:OKJ88450.1}.
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DR EMBL; LIVZ01000003; OKJ88450.1; -; Genomic_DNA.
DR RefSeq; WP_073939717.1; NZ_LIVZ01000003.1.
DR AlphaFoldDB; A0A1Q5L3P5; -.
DR STRING; 1703942.AMK31_08130; -.
DR OrthoDB; 1145at2; -.
DR Proteomes; UP000185813; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000185813}.
FT DOMAIN 15..321
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 344..415
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
FT REGION 413..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 49559 MW; 24AE3A562E7318DB CRC64;
MFGDGSLERF KREGRIVVVG ASLAGLRAAE TLREKGFTGS LTMIGDEPHE PYDRPPLSKQ
VLLGRAAADR TALPRRRSVD ATWRLGVAAT GLDMAARRVR LADGDEVPYD RLLIATGVRA
RPWPREAEAE LDGVFVLRTR DDGAALARRL AEGPERVLVI GAGFTGSEIA SACRERGLSV
TVAERGSAPL VGALGGVVGS VAAELQREHG VDLRCGVMVT ALEGDASGRV RAAQLSDGST
VETDVVIVSL GARRNTDWLA GSGLGAGPRG IACDAGCRAF DFRGIVTDDI YAAGDVARCP
HPLFGYQFLS LEHWGNAVSQ ADIAAHNMLS ESTDRLPHME VPAFWSSQFG VNIKSVGVPS
LGTELLVTQG SLEDHRFVAV YGYQGRVIGA VAFDHARWLP FYQELIERTA PFPPQFPTVD
RRSDGQRPVA ADFPDPSVPT HGPTVTLSGY SPADRRMTFT PAH
//
