ID A0A0R3E3L1_9BRAD Unreviewed; 388 AA.
AC A0A0R3E3L1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Dibenzothiophene monooxygenase {ECO:0000256|ARBA:ARBA00034345};
DE EC=1.14.14.21 {ECO:0000256|ARBA:ARBA00034328};
GN ORFNames=AOQ71_04730 {ECO:0000313|EMBL:KRQ16753.1};
OS Bradyrhizobium manausense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=989370 {ECO:0000313|EMBL:KRQ16753.1, ECO:0000313|Proteomes:UP000051936};
RN [1] {ECO:0000313|EMBL:KRQ16753.1, ECO:0000313|Proteomes:UP000051936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR3351 {ECO:0000313|EMBL:KRQ16753.1,
RC ECO:0000313|Proteomes:UP000051936};
RA De Araujo J.L., Zilli J.E.;
RT "Draft Genome Sequence of Bradyrhizobium manausense Strain BR 3351T, a
RT Novel Symbiotic Nitrogen-Fixing Alphaproteobacterium Isolated from
RT Brazilian Amazon Rain Forest.";
RL Submitted (SEP-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}.
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:KRQ16753.1}.
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DR EMBL; LJYG01000023; KRQ16753.1; -; Genomic_DNA.
DR RefSeq; WP_057742566.1; NZ_LJYG01000023.1.
DR AlphaFoldDB; A0A0R3E3L1; -.
DR STRING; 989370.AOQ71_04730; -.
DR OrthoDB; 6184213at2; -.
DR Proteomes; UP000051936; 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, ECO:0000313|EMBL:KRQ16753.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000313|EMBL:KRQ16753.1}.
FT DOMAIN 16..109
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 125..200
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 228..363
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 388 AA; 42073 MW; E8812A048FD1FA55 CRC64;
MKSRGAGWRS VLSNVRGQLA ETAVARDRSG GTAKAERDLL RRSGLLLLSV PCEYGGIGAS
WIDIFGAVRE LAQVDPSLAH LFAFQHLQIG SILLYASREQ QASLLRGTVE QGWFWGNALN
PRDARTHLTA DGTGFLLDGI KSFCSGARDS DRLLVSTHDA RGGFHIAALP TVREGITVLD
DWDNMGQRQT DSGTVSFERV AVAQHEVLGP PGPFGTRASL RACLAQTVLG MIYLGIAQGA
LEQAITFTRE QSRPWPGSGV ETALEDAYIQ QHYGEFHVAL AGAEALSERA LAQLKAAWDE
GDKLGAEGRG EAAVAIATFK VAAMKAGLDI ATRLFEVTGA RATHARHGFD RYWRNLRTHS
LHDPVDYKLK DLGCFILTGR YPVPGFYS
//
