ID A0A0N1NMY1_9ACTN Unreviewed; 433 AA.
AC A0A0N1NMY1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Ferredoxin--NAD(+) reductase {ECO:0000313|EMBL:KPI21483.1};
DE EC=1.18.1.3 {ECO:0000313|EMBL:KPI21483.1};
GN ORFNames=OK074_1088 {ECO:0000313|EMBL:KPI21483.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI21483.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI21483.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI21483.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-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:KPI21483.1}.
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DR EMBL; LJCV01000033; KPI21483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NMY1; -.
DR PATRIC; fig|1592327.3.peg.871; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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; 2.
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 Oxidoreductase {ECO:0000313|EMBL:KPI21483.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991}.
FT DOMAIN 3..215
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 254..331
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 353..424
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
FT REGION 234..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 44499 MW; 7DD990D48ADD484C CRC64;
MKTVTVVGAS LSGLYAVREL RAQGFDGRLV VVGEEPHRPY DRPPLSKDFL GGRTDEEQLA
LADAEEIAEL DVEWLLGTRA RGLDTRGRTV LLDGGRTVST DGVVIATGAS ARRLPGDDLA
GVHTLRTLDD ARALRAELGG GARRVVVIGG GFIGAETASS CAALGHDVTV VEAAPLPLVP
QLGPEMAAVC AGLHRRGGAT LVTGTGVAGL RSGGTTAAAA ESAAAPAAVW ALSEEPGGAA
PHGGGPHGAA PRRSVTAVEL ADGRVLPADI VIVGIGATPN TGWLAGSTLA LHDGVLCDDG
CATALPQVVA VGDVARVGGV RAEHWTSATE QPRVAVRNLL AGATVETARS LPYFWSDQYG
ARIQFAGRRQ DGDTVRIEEG ALADGAPAEG GFLARYERDG RTTAVLSVDR PRPFMRARRE
LARSGGPVEQ TVS
//
