ID A0A345HQX1_9ACTN Unreviewed; 422 AA.
AC A0A345HQX1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Dibenzothiophene monooxygenase {ECO:0000256|ARBA:ARBA00034345};
DE EC=1.14.14.21 {ECO:0000256|ARBA:ARBA00034328};
GN ORFNames=DVK44_16965 {ECO:0000313|EMBL:AXG79095.1};
OS Streptomyces paludis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2282738 {ECO:0000313|EMBL:AXG79095.1, ECO:0000313|Proteomes:UP000253868};
RN [1] {ECO:0000313|Proteomes:UP000253868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSSD-12 {ECO:0000313|Proteomes:UP000253868};
RA Zhao J.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dibenzothiophene + 2 FMNH2 + 2 O2 = dibenzothiophene 5,5-
CC dioxide + 2 FMN + 2 H(+) + 2 H2O; Xref=Rhea:RHEA:49072,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:23681, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:90356; EC=1.14.14.21;
CC Evidence={ECO:0000256|ARBA:ARBA00034263};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dibenzothiophene + FMNH2 + O2 = dibenzothiophene 5-oxide + FMN
CC + H(+) + H2O; Xref=Rhea:RHEA:49076, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23681,
CC ChEBI:CHEBI:23683, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00034250};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dibenzothiophene 5-oxide + FMNH2 + O2 = dibenzothiophene 5,5-
CC dioxide + FMN + H(+) + H2O; Xref=Rhea:RHEA:49080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23683,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90356;
CC Evidence={ECO:0000256|ARBA:ARBA00034278};
CC -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC {ECO:0000256|ARBA:ARBA00034307}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DszC flavin monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00034317}.
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DR EMBL; CP031194; AXG79095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345HQX1; -.
DR KEGG; spad:DVK44_16965; -.
DR OrthoDB; 571684at2; -.
DR Proteomes; UP000253868; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018640; F:dibenzothiophene monooxygenase activity; IEA:RHEA.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR023922; S04_starv_induced_SfnB.
DR NCBIfam; TIGR04022; sulfur_SfnB; 1.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000313|EMBL:AXG79095.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253868}.
FT DOMAIN 24..125
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 137..235
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 262..397
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 422 AA; 44297 MW; CCD232D343827DE6 CRC64;
MAVRAHVVAQ AVAHVVADDA EALAVAAALA EEFRTGAAAR DAGRVLPRAE LDRLSASGLL
GVTVPRAYGG AEVSARTLAE VFRLLAAADP SLAQIPQSHF VYVNVLRGQG TDAQRKFFFG
EVLAGRRFGN AQSEKGTAHV RDIRTRLVPR GDGAGGDGVL LLNGEKHYAT GALFADWIPV
LARLGGTGDG RHGDGDSPLH VAYVHRDAPG VTVVDDWDGM GQRTTASGTV RLVDVEVAAD
RVVPHHLTFE GPQLHGALAQ LLHAAIDAGI AGGALAEAAA FVRTHSRPWF EAVGEGYGTT
AEDPLLVQRF GELGLDVRAS DAVLRAAADA VDAASADLTD SSAAEASIAV AAAKVHAARA
AVETGSALFE VAGTRAALDG LNLHRYWRDA RTHTLHDPVR WKVQHIGRYV LRGTRPPRHG
LL
//
