DSZC1_RHOER
ID DSZC1_RHOER Reviewed; 417 AA.
AC A0A0C6DRW4;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Dibenzothiophene monooxygenase {ECO:0000303|PubMed:25627402};
DE Short=DBT monooxygenase {ECO:0000303|PubMed:25627402};
DE Short=DBT-MO;
DE EC=1.14.14.21 {ECO:0000269|Ref.2};
GN Name=dszC {ECO:0000303|PubMed:25627402};
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=1833;
RN [1] {ECO:0007744|PDB:3X0X, ECO:0007744|PDB:3X0Y}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS)
RP IN COMPLEX WITH FMN, PATHWAY, SUBUNIT, AND DOMAIN.
RC STRAIN=D-1;
RX PubMed=25627402; DOI=10.1111/febs.13216;
RA Guan L.J., Lee W.C., Wang S., Ohshiro T., Izumi Y., Ohtsuka J.,
RA Tanokura M.;
RT "Crystal structures of apo-DszC and FMN-bound DszC from Rhodococcus
RT erythropolis D-1.";
RL FEBS J. 282:3126-3135(2015).
RN [2]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=D-1;
RX DOI=10.1016/S0922-338X(97)80985-3;
RA Ohshiro T., Suzuki K., Izumi Y.;
RT "Dibenzothiophene (DBT) Degrading Enzyme Responsible for the First Step of
RT DBT Desulfurization by Rhodococcus erythropolis D-l: Purification and
RT Characterization.";
RL J. Ferment. Bioeng. 83:233-237(1997).
RN [3]
RP FUNCTION.
RX PubMed=11229908; DOI=10.1128/aem.67.3.1179-1184;
RA Matsubara T., Ohshiro T., Nishina Y., Izumi Y.;
RT "Purification, characterization, and overexpression of flavin reductase
RT involved in dibenzothiophene desulfurization by Rhodococcus erythropolis D-
RT 1.";
RL Appl. Environ. Microbiol. 67:1179-1184(2001).
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 (Ref.2, PubMed:11229908). Also acts on thioxanthen-9-one and 4,6-
CC dimethyl DBT and 2,8-dimethyl DBT (Ref.2).
CC {ECO:0000269|PubMed:11229908, ECO:0000269|Ref.2}.
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; Evidence={ECO:0000269|Ref.2};
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|Ref.2};
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|Ref.2};
CC -!- COFACTOR:
CC Note=Reduced flavin is provided by flavin reductase DszD.
CC {ECO:0000269|PubMed:11229908};
CC -!- ACTIVITY REGULATION: DBT degradation completely inhibited by Cu(2+),
CC Mn(2+), p-chloromercuribenzoic acid, 2,2-bipyridyl, 1,10-
CC phenanthroline, and strongly inhibited by Zn(2+), 5,5'- Dithiobis(2-
CC nitrobenzoic acid) and 8-quinolinol. {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC {ECO:0000305|PubMed:25627402}.
CC -!- SUBUNIT: Homotetramer formed by a dimer of dimers; FMN binds between
CC monomers of the homodimer. {ECO:0000269|PubMed:25627402}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|Ref.2}.
CC -!- DOMAIN: Has 3 domains, the helical N-terminus (residues 18-124), a
CC beta-barrel central domain (125-233) and a helical C-terminus (234-
CC 417). The lid loop (residues 131-142) change conformation when FMN is
CC bound and close the FMN-binding site. Other regions that probably
CC contribute to FMN binding are residues 178-184 and 281-291.
CC {ECO:0000269|PubMed:25627402}.
CC -!- SIMILARITY: Belongs to the DszC flavin monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; LC027463; BAQ25859.1; -; Genomic_DNA.
DR PDB; 3X0X; X-ray; 2.11 A; A/B/C/D/E/F/G/H=1-417.
DR PDB; 3X0Y; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-417.
DR PDBsum; 3X0X; -.
DR PDBsum; 3X0Y; -.
DR SMR; A0A0C6DRW4; -.
DR KEGG; ag:BAQ25859; -.
DR BRENDA; 1.14.14.21; 5389.
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; Direct protein sequencing; Flavoprotein; FMN;
KW Monooxygenase; Nucleotide-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..417
FT /note="Dibenzothiophene monooxygenase"
FT /id="PRO_0000455397"
FT REGION 18..124
FT /note="Helical N-terminus"
FT /evidence="ECO:0000269|PubMed:25627402"
FT REGION 125..233
FT /note="Central beta-barrel N-terminus"
FT /evidence="ECO:0000269|PubMed:25627402"
FT REGION 131..142
FT /note="Lid loop"
FT /evidence="ECO:0000269|PubMed:25627402"
FT REGION 234..417
FT /note="Helical C-terminus"
FT /evidence="ECO:0000269|PubMed:25627402"
FT BINDING 96
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25627402,
FT ECO:0007744|PDB:3X0Y"
FT BINDING 129..134
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25627402,
FT ECO:0007744|PDB:3X0Y"
FT BINDING 159..163
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25627402,
FT ECO:0007744|PDB:3X0Y"
FT BINDING 282
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25627402,
FT ECO:0007744|PDB:3X0Y"
FT BINDING 369..370
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25627402,
FT ECO:0007744|PDB:3X0Y"
FT BINDING 391
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:25627402,
FT ECO:0007744|PDB:3X0Y"
SQ SEQUENCE 417 AA; 45096 MW; CDBC8C6AE4AEE4B1 CRC64;
MTLSPEKQHV RPRDAADNDP VAVARGLAEK WRATAVERDR AGGSATAERE DLRASGLLSL
LVPREYGGWG ADWPTAIEVV REIAAADGSL GHLFGYHLTN APMIELIGSQ EQEEHLYTQI
AQNNWWTGNA SSENNSHVLD WKVRATPTED 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
