ID F8SXV9_9PSEU Unreviewed; 360 AA.
AC F8SXV9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Tetrahydrofuran monooxygenase reductase component {ECO:0000313|EMBL:AEI99545.1};
GN Name=thmD {ECO:0000313|EMBL:AEI99545.1};
OS Pseudonocardia sp. ENV478.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=377619 {ECO:0000313|EMBL:AEI99545.1};
RN [1] {ECO:0000313|EMBL:AEI99545.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ENV478 {ECO:0000313|EMBL:AEI99545.1};
RA Masuda H., McClay K., Steffan R.J., Zylstra G.J.;
RT "Role of tetrahydrofuran monooxygenase in 1,4-dioxane degradation in
RT Pseudonocardia sp. strain ENV478.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; HQ699618; AEI99545.1; -; Genomic_DNA.
DR AlphaFoldDB; F8SXV9; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; 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 Monooxygenase {ECO:0000313|EMBL:AEI99545.1};
KW Oxidoreductase {ECO:0000313|EMBL:AEI99545.1}.
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 360 AA; 39902 MW; 15C7207CD243288A CRC64;
MGTFNVRFEP IGEEIECGED ETILDAAFRS GLNLVHGCRE GRCSACKAFV LDEGWIYLKK
YSSFALSDQE EEGGYTLLCR AVPESDVTIE LLNYDPDHYR LEHAITDGVG RVVDVEVLTH
DIRRLELQIE SPQSFGFLPG QFVDIWIPGT EQRRSFSMAN LPSDGRLEFI IKQYPGGRFG
AMLDEGLTVG DSVKFTGPYG TCYLRDTGGS RSALLIAGGS GMAPILSLLR QMSEDGQGRT
VSVFYGGRAR RDLFYTELVQ SLGKRIEQFE FIQVVSDESD SDGDDVRCGF VHDAVDQWIE
TSGFRLDACD VYMAGPPPMV DAVNDVLTLR HQVEQNRIFV DKFTSTGPEE SADSDSVSSL
//