ID F2L765_PSEUX Unreviewed; 362 AA.
AC F2L765;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Ferredoxin--NAD(+) reductase {ECO:0000313|EMBL:AEA29038.1};
DE EC=1.18.1.3 {ECO:0000313|EMBL:AEA29038.1};
GN ORFNames=Psed_6977 {ECO:0000313|EMBL:AEA29038.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OG Plasmid pPSED02 {ECO:0000313|EMBL:AEA29038.1}.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA29038.1};
RN [1] {ECO:0000313|EMBL:AEA29038.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CB1190 {ECO:0000313|EMBL:AEA29038.1};
RC PLASMID=pPSED02 {ECO:0000313|EMBL:AEA29038.1};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP002597; AEA29038.1; -; Genomic_DNA.
DR RefSeq; WP_014203927.1; NZ_CP002597.1.
DR RefSeq; YP_004991225.1; NC_016601.1.
DR AlphaFoldDB; F2L765; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Oxidoreductase {ECO:0000313|EMBL:AEA29038.1};
KW Plasmid {ECO:0000313|EMBL:AEA29038.1}.
FT DOMAIN 4..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 105..205
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 362 AA; 40076 MW; 99501455B3FA46DA CRC64;
MGTFNVRFEP IGEEIECGED ETILDAAFRS GLNLVHGCRE GRCSACKAFV LDEGWIYLKK
YSSFALSDQE EEGGYTLLCR AVPESDVTIE LLNYDPDHYR LEHAITDGVG RVVDVEALTH
DIRRLELQIE SPQGFGFLPG QFVDIWIPGT EQRRSFSMAN LPSDGRLEFI IKQYPGGRFG
AMLDEGLTVG DSVKFTGPYG TCYLRDTGGS RSALLIAGGS GMAPILSLLR QMSEDGQGRT
VSVFYGGRAR RDLFYTELVQ SLGKRIEQFE FIQVVSDESD SDGDGDDVRY GFVHDAVDQW
IETSGFRLDA CDVYMAGPPP MVDAVNDVLT LRHQVEQNRI FVDKFTSTGP EESADSDSVS
SL
//
