DSZC_RHOSG
ID DSZC_RHOSG Reviewed; 417 AA.
AC P54998;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Dibenzothiophene monooxygenase {ECO:0000303|PubMed:9634856};
DE Short=DBT monooxygenase;
DE Short=DBT-MO {ECO:0000303|PubMed:9634856};
DE EC=1.14.14.21 {ECO:0000269|PubMed:8824615, ECO:0000269|PubMed:9634856};
DE AltName: Full=DBT sulfur dioxygenase;
DE AltName: Full=Dibenzothiophene desulfurization enzyme C;
DE AltName: Full=Sulfide/sulfoxide monooxygenase {ECO:0000303|PubMed:8824615};
GN Name=dszC {ECO:0000303|PubMed:7574582};
GN Synonyms=soxC {ECO:0000303|PubMed:7961424};
OS Rhodococcus sp. (strain ATCC 53968 / IGTS8).
OG Plasmid pSox.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=54064;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, FLAVIN COFACTOR, PATHWAY,
RP PROBABLE OPERON STRUCTURE, DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 53968 / IGTS8; PLASMID=pSox;
RX PubMed=7961424; DOI=10.1128/jb.176.21.6707-6716.1994;
RA Denome S.A., Oldfield C., Nash L.J., Young K.D.;
RT "Characterization of the desulfurization genes from Rhodococcus sp. strain
RT IGTS8.";
RL J. Bacteriol. 176:6707-6716(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, INDUCTION, PROBABLE
RP OPERON STRUCTURE, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 53968 / IGTS8;
RX PubMed=7574582; DOI=10.1128/aem.61.2.468-475.1995;
RA Piddington C.S., Kovacevich B.R., Rambosek J.;
RT "Sequence and molecular characterization of a DNA region encoding the
RT dibenzothiophene desulfurization operon of Rhodococcus sp. strain IGTS8.";
RL Appl. Environ. Microbiol. 61:468-475(1995).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 53968 / IGTS8;
RX PubMed=8932295; DOI=10.1128/jb.178.22.6409-6418.1996;
RA Li M.Z., Squires C.H., Monticello D.J., Childs J.D.;
RT "Genetic analysis of the dsz promoter and associated regulatory regions of
RT Rhodococcus erythropolis IGTS8.";
RL J. Bacteriol. 178:6409-6418(1996).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, FMNH2 AND NAD COFACTORS, PATHWAY, AND
RP SUBUNIT.
RC STRAIN=ATCC 53968 / IGTS8;
RX PubMed=9634856; DOI=10.1038/nbt1296-1705;
RA Gray K.A., Pogrebinsky O.S., Mrachko G.T., Xi L., Monticello D.J.,
RA Squires C.H.;
RT "Molecular mechanisms of biocatalytic desulfurization of fossil fuels.";
RL Nat. Biotechnol. 14:1705-1709(1996).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, FMNH2 COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 53968 / IGTS8;
RX PubMed=8824615; DOI=10.1128/jb.178.19.5699-5705.1996;
RA Lei B., Tu S.C.;
RT "Gene overexpression, purification, and identification of a desulfurization
RT enzyme from Rhodococcus sp. strain IGTS8 as a sulfide/sulfoxide
RT monooxygenase.";
RL J. Bacteriol. 178:5699-5705(1996).
RN [6]
RP FUNCTION, NADH COFACTOR, PATHWAY, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 53968 / IGTS8;
RX PubMed=9308179; DOI=10.1099/00221287-143-9-2961;
RA Oldfield C., Pogrebinsky O., Simmonds J., Olson E.S., Kulpa C.F.;
RT "Elucidation of the metabolic pathway for dibenzothiophene desulphurization
RT by Rhodococcus sp. strain IGTS8 (ATCC 53968).";
RL Microbiology 143:2961-2973(1997).
RN [7]
RP FUNCTION, PATHWAY, BIOTECHNOLOGY, AND MUTAGENESIS OF VAL-261.
RC STRAIN=ATCC 53968 / IGTS8;
RX PubMed=11823208; DOI=10.1128/aem.68.2.691-698.2002;
RA Arensdorf J.J., Loomis A.K., DiGrazia P.M., Monticello D.J., Pienkos P.T.;
RT "Chemostat approach for the directed evolution of biodesulfurization gain-
RT of-function mutants.";
RL Appl. Environ. Microbiol. 68:691-698(2002).
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. In
CC (PubMed:7961424) DBTO (dibenzothiophene-5-oxide) was reported not to be
CC a substrate, in (PubMed:7574582, PubMed:9634856, PubMed:8824615 and
CC PubMed:9308179) it is reported to be a substrate (PubMed:7961424,
CC PubMed:7574582, PubMed:9634856, PubMed:8824615, PubMed:9308179). Can
CC also use benzyl sulfide and benzyl sulfoxide as substrates, although
CC benzyl sulfoxide is a poor substrate (PubMed:8824615). The pathway
CC substrate specificity has been augmented using mutagenesis, however no
CC mutations allowed use of alkylated thiophenes (PubMed:11823208).
CC {ECO:0000269|PubMed:11823208, ECO:0000269|PubMed:7574582,
CC ECO:0000269|PubMed:7961424, ECO:0000269|PubMed:8824615,
CC ECO:0000269|PubMed:9308179, ECO:0000269|PubMed:9634856}.
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:8824615, ECO:0000269|PubMed:9634856};
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:0000269|PubMed:8824615, ECO:0000269|PubMed:9634856};
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:0000269|PubMed:8824615, ECO:0000269|PubMed:9634856};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:7961424};
CC Note=Addition of FAD increases DBTO2 production in cell lysates.
CC {ECO:0000269|PubMed:7961424};
CC -!- COFACTOR:
CC Name=NADH; Xref=ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:9308179};
CC Note=Reduced flavin is provided by flavin reductase DszD; in vitro
CC NADPH and FAD are not substrates. {ECO:0000269|PubMed:9634856};
CC -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC {ECO:0000269|PubMed:11823208, ECO:0000269|PubMed:7574582,
CC ECO:0000269|PubMed:7961424, ECO:0000269|PubMed:9634856}.
CC -!- SUBUNIT: Homotetramer (PubMed:9634856). Homodimer (PubMed:8824615).
CC {ECO:0000269|PubMed:8824615, ECO:0000269|PubMed:9634856}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expressed during growth on DBT or DMSO as sole sulfur source
CC (at protein level) (PubMed:8932295). Part of the probable dszA-dszB-
CC dszC operon (Probable). Desulfurization is repressed by sulfate,
CC cysteine and methionine (PubMed:7574582, PubMed:8932295).
CC {ECO:0000269|PubMed:7574582, ECO:0000269|PubMed:8932295,
CC ECO:0000305|PubMed:7574582, ECO:0000305|PubMed:7961424,
CC ECO:0000305|PubMed:8932295}.
CC -!- DOMAIN: The lid loop assumes one of 2 conformations allowing opening
CC and closing of the active site. {ECO:0000250|UniProtKB:A0A0C6DRW4}.
CC -!- DISRUPTION PHENOTYPE: No detectable desulfurization activity on DBT.
CC {ECO:0000269|PubMed:7961424}.
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. In addition it may be
CC possible to engineer the operon to make specialty chemicals.
CC {ECO:0000269|PubMed:11823208, ECO:0000269|PubMed:7574582,
CC ECO:0000269|PubMed:7961424, ECO:0000269|PubMed:9308179}.
CC -!- SIMILARITY: Belongs to the DszC flavin monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; U08850; AAA56673.1; -; Genomic_DNA.
DR EMBL; L37363; AAA99484.1; -; Genomic_DNA.
DR AlphaFoldDB; P54998; -.
DR SMR; P54998; -.
DR PRIDE; P54998; -.
DR BioCyc; MetaCyc:MON-264; -.
DR BRENDA; 1.14.14.21; 27672.
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 Cytoplasm; Flavoprotein; FMN; Monooxygenase; Nucleotide-binding;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..417
FT /note="Dibenzothiophene monooxygenase"
FT /id="PRO_0000072048"
FT REGION 131..142
FT /note="Lid loop"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 96
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 129..134
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 159..163
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 282
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 369..370
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 391
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT MUTAGEN 261
FT /note="V->A,Y: Considerable decrease of activity on DBT."
FT /evidence="ECO:0000269|PubMed:11823208"
FT MUTAGEN 261
FT /note="V->C: Decreased activity on DBT."
FT /evidence="ECO:0000269|PubMed:11823208"
FT MUTAGEN 261
FT /note="V->D,E,G,H,K,N,P,Q,R,S,W: Loss of activity on DBT."
FT /evidence="ECO:0000269|PubMed:11823208"
FT MUTAGEN 261
FT /note="V->F: In dszC1; decreased activity on DBT, strain
FT can also use 5-MBT, improved activity against
FT benzothiophene, does not act on octyl sulfide."
FT /evidence="ECO:0000269|PubMed:9308179"
FT MUTAGEN 261
FT /note="V->I,L,M,T: Wild-type activity on DBT."
FT /evidence="ECO:0000269|PubMed:11823208"
FT CONFLICT 56
FT /note="G -> A (in Ref. 2; AAA99484)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="A -> R (in Ref. 2; AAA99484)"
FT /evidence="ECO:0000305"
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
