ID A0A1L3JLB8_9FLAO Unreviewed; 348 AA.
AC A0A1L3JLB8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Flavodoxin reductase {ECO:0000313|EMBL:APG65956.1};
GN ORFNames=LPB136_11540 {ECO:0000313|EMBL:APG65956.1};
OS Tenacibaculum todarodis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1850252 {ECO:0000313|EMBL:APG65956.1, ECO:0000313|Proteomes:UP000181898};
RN [1] {ECO:0000313|EMBL:APG65956.1, ECO:0000313|Proteomes:UP000181898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0136 {ECO:0000313|EMBL:APG65956.1,
RC ECO:0000313|Proteomes:UP000181898};
RA Kim E., Yi H.;
RT "Tenacibaculum sp. LPB0136, isolated from marine environment.";
RL Submitted (NOV-2016) 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; CP018155; APG65956.1; -; Genomic_DNA.
DR RefSeq; WP_072556479.1; NZ_CP018155.1.
DR AlphaFoldDB; A0A1L3JLB8; -.
DR STRING; 1850252.LPB136_11540; -.
DR KEGG; ten:LPB136_11540; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000181898; Chromosome.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06214; PA_degradation_oxidoreductase_like; 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
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 Reference proteome {ECO:0000313|Proteomes:UP000181898}.
FT DOMAIN 2..106
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 258..348
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 348 AA; 38427 MW; 5DAA6031ADA0B304 CRC64;
MNTFYKLKIK ELIQETKDAV SILFSVPSEL KELFSFKAGQ YITIKKELNG EEVRRAYSIC
SSPKSGDLKV AVKAVENGLF SVYATTELKA GDALEVHPPE GKFILNSQAA KNYIAFAAGS
GITPVLSMIK TVLEEESTSK FTLVYGNKMA DSVIFKDELE HLAAAYPNNF KLHTIFSRDK
VKNALQGRID SSVCKYFVKN MYKETTFDSA YLCGPEEMIT AVTETLKDNN FTSENIHFEL
FTASSDEENI GKIKDGETTV TILLDDEETT FTMKQTDDIL AASLRNKVDA PYSCQGGVCS
SCLGKVTEGK AVMTKNSILT DSEVEEGFIL TCQAHPTTPK IVVDFDDV
//
