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Database: UniProt
Entry: M0QI85_9ACTN
LinkDB: M0QI85_9ACTN
Original site: M0QI85_9ACTN 
ID   M0QI85_9ACTN            Unreviewed;       398 AA.
AC   M0QI85;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Dibenzothiophene monooxygenase {ECO:0000256|ARBA:ARBA00034345};
DE            EC=1.14.14.21 {ECO:0000256|ARBA:ARBA00034328};
GN   ORFNames=GS4_05_03560 {ECO:0000313|EMBL:GAC67142.1};
OS   Gordonia soli NBRC 108243.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1223545 {ECO:0000313|EMBL:GAC67142.1, ECO:0000313|Proteomes:UP000011666};
RN   [1] {ECO:0000313|EMBL:GAC67142.1, ECO:0000313|Proteomes:UP000011666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108243 {ECO:0000313|EMBL:GAC67142.1,
RC   ECO:0000313|Proteomes:UP000011666};
RA   Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia soli NBRC 108243.";
RL   Submitted (JAN-2013) 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}.
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:GAC67142.1}.
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DR   EMBL; BANX01000005; GAC67142.1; -; Genomic_DNA.
DR   RefSeq; WP_007618017.1; NZ_BANX01000005.1.
DR   AlphaFoldDB; M0QI85; -.
DR   STRING; 1223545.GS4_05_03560; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 571684at2; -.
DR   Proteomes; UP000011666; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; ISOVALERYL-COA DEHYDROGENASE, 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; 1.
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:0000256|ARBA:ARBA00023033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011666}.
FT   DOMAIN          14..107
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          115..205
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          238..373
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   398 AA;  42381 MW;  14E3DB40D2F757C0 CRC64;
     MTAVISGRDD VLAAIAAGAA ERERNSVDPH AEIRRLADAG LTAFTIGDGT RGSGASVVEL
     IDFVIDLARA DPIVAHILRA HFWFAEQVRR LPVGAERDRW VAEIQAGRIV GNANSERAGA
     AGARRFATQL RPIDGGWLLS GDKFYSTGTA FADWVSVSAS IGGARQDRLA RLVVPVDRPG
     VTVVDDWDGI GQHRTGTGST TFTDVLVTAD DVFEYVDLGT DRATASPSDG PLLQLFLQAV
     ITGILLSVVD DAAELLRGRG RSFDHAPSDE PRHDPVLLRT VGELDSTAHV ARAAVLDAAG
     RIEIAFAGAR VGATDPELFR RASLAAARVK VHVDEVGLRA ASSLFDLGGA SAASRSRNLD
     RHWRNIRTLT LHNPTSYKAI AIGDHVVNGA PLPQNAYF
//
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