ID G5L3J4_9BURK Unreviewed; 339 AA.
AC G5L3J4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=PAHs dioxigenase component ferredoxin reductase {ECO:0000313|EMBL:AER08041.1};
GN Name=dbtAa {ECO:0000313|EMBL:AER08041.1};
OS Burkholderia sp. DBT1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=161152 {ECO:0000313|EMBL:AER08041.1};
RN [1] {ECO:0000313|EMBL:AER08041.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DBT1 {ECO:0000313|EMBL:AER08041.1};
RX PubMed=15068372; DOI=10.1023/B:BIOD.0000015624.52954.b6;
RA Di Gregorio S., Zocca C., Sidler S., Toffanin A., Lizzari D., Vallini G.;
RT "Identification of two new sets of genes for dibenzothiophene
RT transformation in Burkholderia sp. DBT1.";
RL Biodegradation 15:111-123(2004).
RN [2] {ECO:0000313|EMBL:AER08041.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DBT1 {ECO:0000313|EMBL:AER08041.1};
RA Di Gregorio S., Zocca C., Vallini G.;
RL Submitted (OCT-2011) 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; AF404408; AER08041.1; -; Genomic_DNA.
DR AlphaFoldDB; G5L3J4; -.
DR SMR; G5L3J4; -.
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; cd06190; T4MO_e_transfer_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; 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 5..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 105..204
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 339 AA; 37909 MW; DFDBB2688250E551 CRC64;
MTSRSPFNIS LNDSTLSFDV DNGDTILSAA LRNGIGLAYE CNSGGCGNCS FELKDGVVEE
LWAEAPGLSD EARKKGRYLA CQCAPASDLK ISARVNNRFL AQFPPIRFKA PLIAKRMLTS
DMAEFTFRVK EGSDFLPGQF AIFRLPGTDG CRAYSMANLT EDGQFWSFVI KRLPAGRTTN
FLFERLEVGA EIEFDGPYGL SYLQPAIDRD IICIGGGSGL APLLSITRAA IRAPELKHRK
IFFFYGARRS ADHCLKHFLD QDPLIAERVK IIEVVSDEDP EWRGEKGLVH EVLKRQMAGD
LDRYEYYVCG PKGMTDALQV FLSVENKVPT KQIHFDRFY
//
