ID A0A1W9UIX9_9CHLR Unreviewed; 389 AA.
AC A0A1W9UIX9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B6I35_08740 {ECO:0000313|EMBL:OQY21259.1};
OS Anaerolineaceae bacterium 4572_32.2.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae.
OX NCBI_TaxID=1971624 {ECO:0000313|EMBL:OQY21259.1, ECO:0000313|Proteomes:UP000192785};
RN [1] {ECO:0000313|Proteomes:UP000192785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OQY21259.1}.
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DR EMBL; NBLW01000097; OQY21259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9UIX9; -.
DR STRING; 1971624.B6I35_08740; -.
DR Proteomes; UP000192785; Unassembled WGS sequence.
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; cd06217; FNR_iron_sulfur_binding_3; 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; 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; 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}.
FT DOMAIN 50..152
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 306..389
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 389 AA; 43118 MW; A8F5347DAD1C51CA CRC64;
MEIINWLQDV REHVRVSVRR RSLRQPGQGF DYTGDEYRNV VRRVVSAIHP RRMRLCVVEI
VQQTPTTKTF RCERTDGPLP PFRPGQYVNL FVDVDGVLTS RPYSIASAPG SEILELTVRD
NPGGFVAPYL LHEIKVGDEL ETTGPQGHFY HEPLIDGGDL VFLAGGSGIT PFMSIVRDAL
RHERPLNIHL LYGSRAPDDV IYGDELAELA AKHTNFDYTL IISEPPDGYD GVTGFIDAAL
IQEQVGAVTG KTFYICGPQV MYDFCRAALD ELGAPAHKIR RELYGPPADV TREPGWPEGL
AADALFEVDV AGRKTVRAPA GEPLLNTLER YGVVVPAICR SGACSACRVK LLSGKVFQPS
HTGLRESDRE HGYIHACVSY PLEDLRIRL
//
