ID A0A0X3V1Y6_9ACTN Unreviewed; 455 AA.
AC A0A0X3V1Y6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Ferredoxin reductase {ECO:0000313|EMBL:KUL38805.1};
GN ORFNames=ADL22_16130 {ECO:0000313|EMBL:KUL38805.1};
OS Streptomyces sp. NRRL F-4489.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL38805.1, ECO:0000313|Proteomes:UP000053256};
RN [1] {ECO:0000313|EMBL:KUL38805.1, ECO:0000313|Proteomes:UP000053256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL38805.1,
RC ECO:0000313|Proteomes:UP000053256};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KUL38805.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LLZI01000221; KUL38805.1; -; Genomic_DNA.
DR RefSeq; WP_066979191.1; NZ_LLZI01000221.1.
DR AlphaFoldDB; A0A0X3V1Y6; -.
DR STRING; 1609095.ADL22_16130; -.
DR OrthoDB; 1145at2; -.
DR Proteomes; UP000053256; 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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053256}.
FT DOMAIN 9..314
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 337..407
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
FT REGION 403..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 48068 MW; 5C88238EB9A5DEF6 CRC64;
MSGELTRGRI VIVGASLAGL RAAETLRAEG FTGELTVVGD EPHPPYDRPP LSKQVLLGRV
PAADTGLPAR RPVDAHWKLG VRASGVDPDA KEVLLADGER LPFDRLLIAT GTRARPWPNP
EEARLDGVLT VRTMDDAARL AERLDAGPRR VLVIGAGFTG SEIASACRER GLPVTVAERG
PAPLVGALGG TLGAFAARLQ RAHGVDLRCG VTVTTLLGSG GRLTGAEFSD GSRIEADVAV
VALGAVRNTE WLADSGLAAG PRGLACDAGC RAFTMYGIVT DDVFVAGDVA RFPHPLFEYQ
MLSLEHWGNA VAQAEVAAHN MVSPGPRRRP HLAVPAFWSS QFGLNIKSVG VPTFSDQVTI
AQGSVEEGRL VVVYGYRGRI TAAVSVNRAK WLEHYQRLIE TAAPFPPPPG AADRPEAPRV
VPSDVPDPKV LSHGPTVALT GHLPDRRLSL VRPAG
//
