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Database: UniProt
Entry: H5TZU0_9ACTN
LinkDB: H5TZU0_9ACTN
Original site: H5TZU0_9ACTN 
ID   H5TZU0_9ACTN            Unreviewed;       402 AA.
AC   H5TZU0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Dibenzothiophene monooxygenase {ECO:0000256|ARBA:ARBA00034345};
DE            EC=1.14.14.21 {ECO:0000256|ARBA:ARBA00034328};
GN   ORFNames=GOSPT_054_00310 {ECO:0000313|EMBL:GAB38998.1};
OS   Gordonia sputi NBRC 100414.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1089453 {ECO:0000313|EMBL:GAB38998.1, ECO:0000313|Proteomes:UP000005845};
RN   [1] {ECO:0000313|EMBL:GAB38998.1, ECO:0000313|Proteomes:UP000005845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100414 {ECO:0000313|EMBL:GAB38998.1,
RC   ECO:0000313|Proteomes:UP000005845};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia sputi NBRC 100414.";
RL   Submitted (FEB-2012) 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:GAB38998.1}.
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DR   EMBL; BAFC01000054; GAB38998.1; -; Genomic_DNA.
DR   RefSeq; WP_005205408.1; NZ_BAFC01000054.1.
DR   AlphaFoldDB; H5TZU0; -.
DR   eggNOG; COG1960; Bacteria.
DR   Proteomes; UP000005845; 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}.
FT   DOMAIN          12..110
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          116..209
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          243..377
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   402 AA;  42426 MW;  A695691A03319718 CRC64;
     MTAATRVVAD RAAVLAEIAA GSAERERAGE DPRAQIELLR DAGLTALTLD AEHGGGGADV
     VELVEFIVDL ARADPIAAHI LRAHYWFVEQ IKRLPDGPVR DRWSALIADG AVFGNATSER
     AGSAGARRFA TTIRPTDTGW VLSGEKFYST GTAFADFIAV QATVDDAQGG ERLARLIVPV
     DRAGVSVIDD WDGIGQHRTG TGSTQFTDVV VTADDILGIV DLAAPGAPRI ANDAPLLQLF
     LQALITGILL SVNDDAIELV RGRTRTFDHA PADEPRHDPV LLKTIGEIDA AAHVARAAVL
     AAARDVEAAF ECARQGVIDA TLFERASVAA ARVKVHVDSV ALPTATALFD VGGASSASRA
     CNLDRHWRNI RTITLHNPTS YKAIALGDLA VNGTTLPANG YF
//
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