DSZC_RHOSH
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 03-AUG-2022, entry version 72.
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; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC 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 -!- COFACTOR:
CC Note=Reduced flavin is provided by flavin reductase DszD.
CC {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 -!- SIMILARITY: Belongs to the DszC flavin monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AY278323; AAP33510.1; -; Genomic_DNA.
DR PDB; 4DOY; X-ray; 1.79 A; A/B/C/D/E/F/G/H=1-417.
DR PDBsum; 4DOY; -.
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 Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 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.
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 SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 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"
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
