ID A0A3A4F881_9MICC Unreviewed; 417 AA.
AC A0A3A4F881;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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=D3250_02365 {ECO:0000313|EMBL:RJN32690.1};
OS Nesterenkonia natronophila.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Nesterenkonia.
OX NCBI_TaxID=2174932 {ECO:0000313|EMBL:RJN32690.1, ECO:0000313|Proteomes:UP000266615};
RN [1] {ECO:0000313|EMBL:RJN32690.1, ECO:0000313|Proteomes:UP000266615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:RJN32690.1,
RC ECO:0000313|Proteomes:UP000266615};
RA Menes R.J., Iriarte A.;
RT "Nesterenkonia natronophila sp. nov., an alkaliphilic actinobacteriume
RT isolated from a soda lake, and emended description of the genus
RT Nesterenkonia.";
RL Submitted (SEP-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}.
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:RJN32690.1}.
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DR EMBL; QYZP01000001; RJN32690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A4F881; -.
DR OrthoDB; 571684at2; -.
DR Proteomes; UP000266615; Unassembled WGS sequence.
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; 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; 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; 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:UP000266615}.
FT DOMAIN 25..117
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 124..212
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 242..385
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 417 AA; 44735 MW; C7E132AFBBCB7DA8 CRC64;
MGGGEPMKTT ADQHTLLPGD LLETIASGAV ERELHRILPF EEVRLLDECG FGALRVPTEH
GGPGLSVEQL IGEVIALARA DSNIAHLYRG HFGFVESLRF QPPEIQKAWY PRVLKGKTVG
NASTERGGNA LGTLNTTLTA GEDGWVLNGE KFYSTGTIFS DYTRVSASQE DGDKGRRFAV
VPRDAAGVTV ADDWDGFGQK LTGTGTTVFE DVVVSPLSLL NRSYGSHEAV HEAAFFQLYL
LAVQVGIAHA AVRDAANLLR RRTRTFNTSA TGAAFKQDPL IQQVVGRMSA KAFVAQAAVV
EVARIHDQAL RSGLAAGTQR ASHRGELPAD VYSAEIAVQQ AQVTVPDLVL AVTQELFQTV
GASATLRSKA LDRHWRNAQT IATHNPIVFR ARSIGDYEVN GTLPEGLNAI GESGASR
//
