ID A0A1H2MWR6_9PSED Unreviewed; 337 AA.
AC A0A1H2MWR6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Benzoate/toluate 1,2-dioxygenase reductase subunit {ECO:0000313|EMBL:SDU97398.1};
GN ORFNames=SAMN05216202_2500 {ECO:0000313|EMBL:SDU97398.1};
OS Pseudomonas mucidolens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=46679 {ECO:0000313|EMBL:SDU97398.1, ECO:0000313|Proteomes:UP000198600};
RN [1] {ECO:0000313|Proteomes:UP000198600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 2223 {ECO:0000313|Proteomes:UP000198600};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
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DR EMBL; LT629802; SDU97398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2MWR6; -.
DR STRING; 46679.SAMN05216202_2500; -.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000198600; Chromosome i.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06209; BenDO_FAD_NAD; 1.
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; IPR047683; BenC-like_FAD_NAD-bd.
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 NCBIfam; NF040810; BenC; 1.
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 Dioxygenase {ECO:0000313|EMBL:SDU97398.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Oxidoreductase {ECO:0000313|EMBL:SDU97398.1}.
FT DOMAIN 3..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 104..204
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 337 AA; 36465 MW; 13F5876E5285C82F CRC64;
MTHSIAFNFE DGVTRFIDAN AGETVADAAY RQGINIPLDC RDGACGTCKC FAEAGRYDLG
EDYIEDALSA DEAQQGFVLT CQMRAQSDCV VRVPVSSDVC RTRQASYDAT ISAVRQLSDS
TIALSIKGEA LSKLAFLPGQ YVNLGVPGSE QTRAYSFSSL QRDGEVSFLI RNVPGGLMSS
FLTGMAKAGD SMSLAGPLGS FYLRDIRRPL LLLAGGTGLA PFTAMLERIA EQGSEHPLHL
IYGVTNDFDL VELDRLEAFA ARIPNFSFSA CVANPDSRHP LKGYVTQHIE PRHLNDGDVD
VYLCGPPPMV EAVSQFIREQ GIAPVNFYYE KFAASAA
//