ID B8HLR6_CYAP4 Unreviewed; 383 AA.
AC B8HLR6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Dibenzothiophene monooxygenase {ECO:0000256|ARBA:ARBA00034345};
DE EC=1.14.14.21 {ECO:0000256|ARBA:ARBA00034328};
GN OrderedLocusNames=Cyan7425_1173 {ECO:0000313|EMBL:ACL43554.1};
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC Cyanothece.
OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL43554.1};
RN [1] {ECO:0000313|EMBL:ACL43554.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL43554.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L.,
RA Sato H., Zhao L., Sherman L., Pakrasi H., Richardson P.;
RT "Complete sequence of chromosome Cyanothece sp. PCC 7425.";
RL Submitted (JAN-2009) 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; CP001344; ACL43554.1; -; Genomic_DNA.
DR AlphaFoldDB; B8HLR6; -.
DR STRING; 395961.Cyan7425_1173; -.
DR KEGG; cyn:Cyan7425_1173; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_2_3; -.
DR OrthoDB; 9785203at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..103
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 129..216
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 251..360
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 383 AA; 41236 MW; 14EAB81E87B9FC97 CRC64;
MLTLEIEPTV KQGENDWLSL AESLGKQFAE KEAIADAGDL FVADNIAQLK SSGLTAAGVP
TELGGGGASF TDLCTVLNIL GRYSSSTALA FSMHTHQVMV PTWRWQHQHA PVDGFLKRVA
TEQLILVSSG GSDWLQSGGT ATKVEGGFRV TARKVFASGA PAGDLLITSA VYADPEQGAT
VLHFAIPLKA AGVEIEPTWQ ALGMRGTGSH DVVCSDIFIP DAAVTLRREQ GKWHFIFHLI
SMIAIPLVYS VYVGVAEAAR DRVLQLARKH PNTEHLYYMV GGLDNELMAA KLALQQMIAT
AVTSQPGFET TNQIMTGRTL VAKAVLNVAD LAMEIAGGSA FYRKLGLEKL FRDLQGVRYH
PLREEAQRKL AGQLALGYDT SSL
//
