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Entry: A0A0N9I5W2_9PSEU
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ID   A0A0N9I5W2_9PSEU        Unreviewed;       371 AA.
AC   A0A0N9I5W2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Dibenzothiophene monooxygenase {ECO:0000256|ARBA:ARBA00034345};
DE            EC=1.14.14.21 {ECO:0000256|ARBA:ARBA00034328};
GN   ORFNames=AOZ06_47405 {ECO:0000313|EMBL:ALG13484.1};
OS   Kibdelosporangium phytohabitans.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kibdelosporangium.
OX   NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG13484.1, ECO:0000313|Proteomes:UP000063699};
RN   [1] {ECO:0000313|EMBL:ALG13484.1, ECO:0000313|Proteomes:UP000063699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG13484.1,
RC   ECO:0000313|Proteomes:UP000063699};
RA   Qin S., Xing K.;
RT   "Genome sequencing of Kibdelosporangium phytohabitans.";
RL   Submitted (JUL-2015) 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; CP012752; ALG13484.1; -; Genomic_DNA.
DR   RefSeq; WP_054295372.1; NZ_JADBEI010000001.1.
DR   AlphaFoldDB; A0A0N9I5W2; -.
DR   STRING; 860235.AOZ06_47405; -.
DR   KEGG; kphy:AOZ06_47405; -.
DR   OrthoDB; 571684at2; -.
DR   Proteomes; UP000063699; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; 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   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:UP000063699}.
FT   DOMAIN          112..183
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          215..345
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   371 AA;  39452 MW;  73879BFB17CD169A CRC64;
     MTDWIGLAEE VAARLKADAA ERDRANRPPT AEVDLLRSSG LLAADESAAD AVTRIIAAAD
     ASIGHLIGYH YLHLWRARLF DNPAAAQRMR ADANWFWSGV SNPLDAALRL TPSGDGFIVN
     GRKTFATGAS VADRLVVSAT RVDNDEKVTF TVDAKASGIS YPSDWDNTGQ RLTASGGIVF
     EDVAVDGQDV LGPQPSDSIR LSLAALGFQL ALTQIYVGIA AGALAEAAEY TRGQARPWIL
     SGVESASADP YIAAGYGELV ASVEAAGTLA DRAADALRQS VDAGAELTAE LRASTAVTIS
     SAKVFATRVV NETTTKVFEF MGARATATKF GYDRFWRNAR TLTLHDPVVY KAREVGAYYL
     TGEHPPFTGY S
//
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