ID DSZC_RHOSH Reviewed; 417 AA. AC Q6WNP1; DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 79. DE RecName: Full=Dibenzothiophene monooxygenase {ECO:0000303|PubMed:24470304}; DE Short=DBT monooxygenase {ECO:0000305}; DE Short=DBT-MO {ECO:0000305}; DE EC=1.14.14.21 {ECO:0000269|PubMed:24470304}; DE AltName: Full=Dibenzothiophene desulfurization enzyme C {ECO:0000303|PubMed:16820450}; GN Name=dszC {ECO:0000303|PubMed:16820450}; OS Rhodococcus erythropolis (strain XP). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Rhodococcus; Rhodococcus erythropolis group. OX NCBI_TaxID=1078016; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE FUNCTION, PATHWAY, AND RP BIOTECHNOLOGY. RC STRAIN=XP; RX PubMed=16820450; DOI=10.1128/aem.00081-06; RA Tao F., Yu B., Xu P., Ma C.Q.; RT "Biodesulfurization in biphasic systems containing organic solvents."; RL Appl. Environ. Microbiol. 72:4604-4609(2006). RN [2] {ECO:0007744|PDB:4DOY} RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF HIS-92; TYR-96; ASN-129; PHE-161; RP SER-163; TRP-205; ARG-282; ARG-370; HIS-388; HIS-391 AND ASP-392. RC STRAIN=XP; RX PubMed=24470304; DOI=10.1002/prot.24525; RA Liu S., Zhang C., Su T., Wei T., Zhu D., Wang K., Huang Y., Dong Y., RA Yin K., Xu S., Xu P., Gu L.; RT "Crystal structure of DszC from Rhodococcus sp. XP at 1.79 A."; RL Proteins 82:1708-1720(2014). CC -!- FUNCTION: Catalyzes the first step of the '4S' desulfurization pathway CC that removes covalently bound sulfur from dibenzothiophene (DBT) CC without breaking carbon-carbon bonds. Sulfur dioxygenase which converts CC DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner. CC {ECO:0000305|PubMed:16820450}. 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:0000269|PubMed:24470304}; 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:0000305|PubMed:24470304}; 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:0000305|PubMed:24470304}; CC -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation. CC {ECO:0000269|PubMed:16820450}. CC -!- SUBUNIT: Homotetramer formed of a dimer of dimers. CC {ECO:0000269|PubMed:24470304}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The lid loop assumes one of 2 conformations allowing opening CC and closing of the active site; in the 3D structure one dimer is open CC while the other is closed (PubMed:24470304). Another structure with FMN CC (3X0Y) proposes a different lid loop that may interact with the loop CC predicted here (By similarity). {ECO:0000250|UniProtKB:A0A0C6DRW4, CC ECO:0000269|PubMed:24470304, ECO:0007744|PDB:4DOY}. CC -!- BIOTECHNOLOGY: Can be used to remove sulfur from polycyclic aromatic CC sulfur compounds found in gasoline and diesel (biodesulfurization), CC which are a considerable source of pollution. As the substrates are not CC very soluble in conventional media, biphasic systems may help improve CC catalysis. Expression of dszD-dszA-dszB-dszC (cloned in this order) in CC organic-solvent-tolerant P.putida strain Idaho allows P.putida to grow CC on 10% p-xylene with DBT as the sole sulfur source. In this P.putida CC strain 97% of DBT was degraded, 71% of 4,6-dimethyldibenzothiophene and CC about 50% of 3-methyldibenzothiophene or 4-methyldibenzothiophene was CC degraded in the presence of 10% p-xylene. Degradation of DBT in the CC presence of 10% of other organic solvents was tested; when grown in CC dodecane, cyclohexane or heptanol bacteria metabolized DBT as well as CC p-xylene, while other organic solvents degraded DBT slightly less well. CC {ECO:0000269|PubMed:16820450}. CC -!- MISCELLANEOUS: Reduced flavin is provided by flavin reductase DszD. CC {ECO:0000305|PubMed:24470304}. CC -!- SIMILARITY: Belongs to the DszC flavin monooxygenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY278323; AAP33510.1; -; Genomic_DNA. DR RefSeq; WP_019750078.1; NZ_AGCF01000009.1. DR PDB; 4DOY; X-ray; 1.79 A; A/B/C/D/E/F/G/H=1-417. DR PDBsum; 4DOY; -. DR AlphaFoldDB; Q6WNP1; -. DR SMR; Q6WNP1; -. DR BRENDA; 1.14.14.21; 5397. DR UniPathway; UPA00346; -. 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 GO; GO:0018896; P:dibenzothiophene catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd01163; DszC; 1. 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Flavoprotein; FMN; Monooxygenase; KW Nucleotide-binding; Oxidoreductase. FT CHAIN 1..417 FT /note="Dibenzothiophene monooxygenase" FT /id="PRO_0000455399" FT REGION 131..142 FT /note="First lid loop" FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4" FT REGION 280..295 FT /note="Second lid loop" FT /evidence="ECO:0000269|PubMed:24470304" FT BINDING 92 FT /ligand="dibenzothiophene" FT /ligand_id="ChEBI:CHEBI:23681" FT /evidence="ECO:0000305|PubMed:24470304" FT BINDING 96 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4, FT ECO:0000305|PubMed:24470304" FT BINDING 129..134 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4" FT BINDING 129 FT /ligand="dibenzothiophene" FT /ligand_id="ChEBI:CHEBI:23681" FT /evidence="ECO:0000305|PubMed:24470304" FT BINDING 159..163 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4, FT ECO:0000305|PubMed:24470304" FT BINDING 205 FT /ligand="dibenzothiophene" FT /ligand_id="ChEBI:CHEBI:23681" FT /evidence="ECO:0000305|PubMed:24470304" FT BINDING 282 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4, FT ECO:0000305|PubMed:24470304" FT BINDING 369..370 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4, FT ECO:0000305|PubMed:24470304" FT BINDING 391..392 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000305|PubMed:24470304" FT BINDING 391 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4" FT MUTAGEN 92 FT /note="H->F: No production of DBTO2 from DBT." FT /evidence="ECO:0000269|PubMed:24470304" FT MUTAGEN 96 FT /note="Y->A: No production of DBTO2 from DBT." FT /evidence="ECO:0000269|PubMed:24470304" FT MUTAGEN 129 FT /note="N->A: Almost no production of DBTO2 from DBT." FT /evidence="ECO:0000269|PubMed:24470304" FT MUTAGEN 161 FT /note="F->A: No production of DBTO2 from DBT." FT /evidence="ECO:0000269|PubMed:24470304" FT MUTAGEN 163 FT /note="S->A: No production of DBTO2 from DBT." FT /evidence="ECO:0000269|PubMed:24470304" FT MUTAGEN 205 FT /note="W->A: No production of DBTO2 from DBT." FT /evidence="ECO:0000269|PubMed:24470304" FT MUTAGEN 282 FT /note="R->A: Almost no production of DBTO2 from DBT." FT /evidence="ECO:0000269|PubMed:24470304" FT MUTAGEN 370 FT /note="R->A: Almost no production of DBTO2 from DBT." FT /evidence="ECO:0000269|PubMed:24470304" FT MUTAGEN 388 FT /note="H->F: Very little production of DBTO2 from DBT." FT /evidence="ECO:0000269|PubMed:24470304" FT MUTAGEN 391 FT /note="H->F: Very little production of DBTO2 from DBT." FT /evidence="ECO:0000269|PubMed:24470304" FT MUTAGEN 392 FT /note="D->N: Very little production of DBTO2 from DBT." FT /evidence="ECO:0000269|PubMed:24470304" FT HELIX 20..32 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 35..41 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 46..55 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 73..86 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 88..100 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 102..107 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 110..123 FT /evidence="ECO:0007829|PDB:4DOY" FT STRAND 127..130 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:4DOY" FT STRAND 144..147 FT /evidence="ECO:0007829|PDB:4DOY" FT STRAND 153..161 FT /evidence="ECO:0007829|PDB:4DOY" FT STRAND 169..176 FT /evidence="ECO:0007829|PDB:4DOY" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:4DOY" FT TURN 182..185 FT /evidence="ECO:0007829|PDB:4DOY" FT STRAND 187..193 FT /evidence="ECO:0007829|PDB:4DOY" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:4DOY" FT STRAND 218..225 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 227..229 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 236..243 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 246..249 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 250..279 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 292..294 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 296..328 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 329..332 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 335..367 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 369..372 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 380..388 FT /evidence="ECO:0007829|PDB:4DOY" FT HELIX 394..407 FT /evidence="ECO:0007829|PDB:4DOY" SQ SEQUENCE 417 AA; 45027 MW; CDBCFC0054AE2FD0 CRC64; MTLSPEKQHV RPRDAADNDP VAVARGLAEK WRATAVERDR AGGSATAERE DLRASGLLSL LVPREYGGWG ADWPTAIEVV REIAAADGSL GHLFGYHLTN APMIELIGSQ EQEEHLYTQI AQNNWWTGNA SSENNSHVLD WKVSATPTED GGYVLNGTKH FCSGAKGSDL LFVFGVVQDD SPQQGAIIAA AIPTSRAGVT PNDDWAAIGM RQTDSGSTDF HNVKVEPDEV LGAPNAFVLA FIQSERGSLF APIAQLIFAN VYLGIAHGAL DAAREYTRTQ ARPWTPAGIQ QATEDPYTIR SYGEFTIALQ GADAAAREAA HLLQTVWDKG DALTPEDRGE LMVKVSGVKA LATNAALNIS SGVFEVIGAR GTHPRYGFDR FWRNVRTHSL HDPVSYKIAD VGKHTLNGQY PIPGFTS //