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Entry: A0A0C4WHQ6_9GAMM
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ID   A0A0C4WHQ6_9GAMM        Unreviewed;       401 AA.
AC   A0A0C4WHQ6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Dibenzothiophene monooxygenase {ECO:0000256|ARBA:ARBA00034345};
DE            EC=1.14.14.21 {ECO:0000256|ARBA:ARBA00034328};
GN   ORFNames=Achr_17160 {ECO:0000313|EMBL:AJE21173.1};
OS   Azotobacter chroococcum NCIMB 8003.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=1328314 {ECO:0000313|EMBL:AJE21173.1, ECO:0000313|Proteomes:UP000068210};
RN   [1] {ECO:0000313|EMBL:AJE21173.1, ECO:0000313|Proteomes:UP000068210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 8003 {ECO:0000313|EMBL:AJE21173.1,
RC   ECO:0000313|Proteomes:UP000068210};
RX   PubMed=26061173;
RA   Robson R.L., Jones R., Robson R.M., Schwartz A., Richardson T.H.;
RT   "Azotobacter Genomes: The Genome of Azotobacter chroococcum NCIMB 8003
RT   (ATCC 4412).";
RL   PLoS ONE 10:E0127997-E0127997(2015).
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; CP010415; AJE21173.1; -; Genomic_DNA.
DR   RefSeq; WP_039803573.1; NZ_CP010415.1.
DR   AlphaFoldDB; A0A0C4WHQ6; -.
DR   STRING; 1328314.Achr_17160; -.
DR   KEGG; acx:Achr_17160; -.
DR   HOGENOM; CLU_018204_10_1_6; -.
DR   Proteomes; UP000068210; Chromosome.
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   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:UP000068210}.
FT   DOMAIN          12..88
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          129..202
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          235..375
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   401 AA;  44110 MW;  77E250017091ABDE CRC64;
     MGTPTTAEDW LALAREIGEE FTRDITRRTR TRERPDAQLR RLKDSGLTNL AIPRELGGAG
     QRWSLIVRTI RELAAGDGSV GMLYGYHQLN LVNLRREPQP RRDRLLAEIA ERRLWLAGVV
     NPRDDDILAT PDGEGFRLDG RKGFCSGAAF ADLLSVSARH ARDGRRLMAL IPADRPGLHY
     ADDWDHFGVE RSDSGSFVLS EVRAEPGEVI ANDLEDGDDF SAVIRTPVNQ SAFTQFYLGS
     ALGALRAARA YVHREGRAGL HAGVDKAHQD PLLVSQFGEL WIALQGAIAL ADRAALKVDE
     LLAADEAFSA ELRGEAAVEV ASGEAAVEVA SAKVLAARTA LDVTSRVFEV MGARATHNRY
     AFDRFWRDTR THSLHDPLAH KLLEVGEYAL NGQYPPVRAY T
//
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