ID Q2J8G1_FRACC Unreviewed; 411 AA.
AC Q2J8G1;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ABD12431.1};
GN OrderedLocusNames=Francci3_3074 {ECO:0000313|EMBL:ABD12431.1};
OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD12431.1, ECO:0000313|Proteomes:UP000001937};
RN [1] {ECO:0000313|EMBL:ABD12431.1, ECO:0000313|Proteomes:UP000001937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45818 / CECT 9043 / CcI3
RC {ECO:0000313|Proteomes:UP000001937};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000249; ABD12431.1; -; Genomic_DNA.
DR RefSeq; WP_011437459.1; NZ_JENI01000022.1.
DR AlphaFoldDB; Q2J8G1; -.
DR STRING; 106370.Francci3_3074; -.
DR KEGG; fra:Francci3_3074; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_4_0_11; -.
DR OrthoDB; 1145at2; -.
DR PhylomeDB; Q2J8G1; -.
DR Proteomes; UP000001937; 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; PR00469; PNDRDTASEII.
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:UP000001937}.
FT DOMAIN 3..292
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 313..407
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 411 AA; 42833 MW; 0CCB2B3166EBBBE9 CRC64;
MQRIVVVGAG MAGGRAAAEV RARGFAGEVI LLGAEPHRPY DRPPLSKAVL SGRIDDTTLP
FDLDGVEVRL GRRATGLRPG TVETDAGPLD YDGLVLATGA DPVTLPGDGP QRVLRSIDDA
RDLRGALRPG VRLVIVGAGW IGAEVATAAA AIGAEVTVVE AAASPLFAAL GAQVGRCTIA
WYARAGVTLR LATAVERVTP DGLVLAGGEE LIADEVVVGV GVRPGTAWLA GSGLALDRGV
VVDEHLAARW THGADGADGD RPPVVAVGDC AAWWSRRYGR RLRVEHWDCA QQSPAVAVST
LLGGEAVYDP VPYFWSEQFG RMVQFAGLPS AEAAPVFRGD PGVVVPPDGG RPSGWSAGWF
APDGRLEALV TVGRPMDMVA GRRLMAADGI PDRERFADIS VSMKELAAAS R
//
