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Database: UniProt
Entry: Q0PHL7_9RALS
LinkDB: Q0PHL7_9RALS
Original site: Q0PHL7_9RALS 
ID   Q0PHL7_9RALS            Unreviewed;       354 AA.
AC   Q0PHL7;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=BtxF {ECO:0000313|EMBL:ABG82171.1};
GN   Name=btxF {ECO:0000313|EMBL:ABG82171.1};
OS   Ralstonia sp. PHS1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=119276 {ECO:0000313|EMBL:ABG82171.1};
RN   [1] {ECO:0000313|EMBL:ABG82171.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PHS1 {ECO:0000313|EMBL:ABG82171.1};
RA   Lee S.K., Lee S.B.;
RT   "Nucleotide sequence and functional analysis of the btx operon for
RT   catabolism of BTEX compounds in Ralstonia sp. strain PHS1.";
RL   Submitted (JUN-2006) 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; DQ834383; ABG82171.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0PHL7; -.
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   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}.
FT   DOMAIN          3..93
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          102..204
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   354 AA;  39161 MW;  8F45AB35BA8A46FF CRC64;
     MTYQLNIQPL GATIEVEEGQ TILDAALRQG IYIPHACGHG LCGTCKVQVC DGEVDLGDAN
     PFALMDFERE ERKALACCAT LLDDTTIEAD IEEDPDAEVI PVEDFNAEVT RIEQLTPTIK
     AVFLRLDQPI HFQAGQYVQL EIPELRQTRA FSIANSPADV AATGEIELNI RRVPGGQGTG
     YIHEQLAVGN ILHVTGPYGR FFVRRSADQP MVFMAGGSGL SSPRSMIIDL LQSGWSRPIT
     LVYGQRNEAE LYYDEEFREL SQRYSNFSYV PALSEKAEGA THPLAQGFVH EVAKAHFGNN
     FSGHKAYLCG PPAMIDACVT TLIQGRLFER DIYFEKFISA ADAQQVRSPL FKRV
//
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