DSZC3_RHOER
ID DSZC3_RHOER Reviewed; 417 AA.
AC Q0ZIH5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Dibenzothiophene monooxygenase {ECO:0000303|PubMed:23722833};
DE Short=DBT monooxygenase {ECO:0000303|PubMed:24975806};
DE Short=DBT-MO;
DE EC=1.14.14.21 {ECO:0000269|PubMed:24975806, ECO:0000305|PubMed:16810451};
GN Name=dszC {ECO:0000303|PubMed:16810451};
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=1833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE FUNCTION, PATHWAY, EXPRESSION
RP IN B.SUBTILIS, INDUCTION, AND BIOTECHNOLOGY.
RC STRAIN=DS-3;
RX PubMed=16810451; DOI=10.1007/s10529-006-9056-0;
RA Ma T., Li G., Li J., Liang F., Liu R.;
RT "Desulfurization of dibenzothiophene by Bacillus subtilis recombinants
RT carrying dszABC and dszD genes.";
RL Biotechnol. Lett. 28:1095-1100(2006).
RN [2]
RP INDUCTION, AND BIOTECHNOLOGY.
RC STRAIN=DS-3;
RX PubMed=17420595; DOI=10.1271/bbb.60189;
RA Li G.Q., Ma T., Li S.S., Li H., Liang F.L., Liu R.L.;
RT "Improvement of dibenzothiophene desulfurization activity by removing the
RT gene overlap in the dsz operon.";
RL Biosci. Biotechnol. Biochem. 71:849-854(2007).
RN [3]
RP BIOTECHNOLOGY.
RC STRAIN=DS-3;
RX PubMed=18165370; DOI=10.1128/aem.02319-07;
RA Li G.Q., Li S.S., Zhang M.L., Wang J., Zhu L., Liang F.L., Liu R.L., Ma T.;
RT "Genetic rearrangement strategy for optimizing the dibenzothiophene
RT biodesulfurization pathway in Rhodococcus erythropolis.";
RL Appl. Environ. Microbiol. 74:971-976(2008).
RN [4] {ECO:0007744|PDB:4JEK}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), AND SUBUNIT.
RC STRAIN=DS-3;
RX PubMed=23722833; DOI=10.1107/s1744309113011172;
RA Duan X., Zhang L., Zhou D., Ji K., Ma T., Shui W., Li G., Li X.;
RT "Crystallization and preliminary structural analysis of dibenzothiophene
RT monooxygenase (DszC) from Rhodococcus erythropolis.";
RL Acta Crystallogr. F 69:597-601(2013).
RN [5] {ECO:0007744|PDB:4NXL}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF TYR-96; ASN-129; PHE-161; SER-163;
RP TRP-205; SER-215; PHE-250; ARG-338; HIS-391; 409-GLN--SER-417; PHE-415;
RP THR-416 AND SER-417.
RC STRAIN=DS-3;
RX PubMed=24975806; DOI=10.1002/prot.24638;
RA Zhang L., Duan X., Zhou D., Dong Z., Ji K., Meng W., Li G., Li X., Yang H.,
RA Ma T., Rao Z.;
RT "Structural insights into the stabilization of active, tetrameric DszC by
RT its C-terminus.";
RL Proteins 82:2733-2743(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:0000269|PubMed:24975806, ECO:0000305|PubMed:16810451}.
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:24975806};
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:24975806};
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:24975806};
CC -!- COFACTOR:
CC Note=Reduced flavin is provided by flavin reductase DszD.
CC {ECO:0000269|PubMed:24975806};
CC -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC {ECO:0000269|PubMed:16810451}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23722833,
CC ECO:0000269|PubMed:24975806}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Repressed by HBP or sulfate (Probable). Part of the dszA-
CC dszB-dszC operon. This protein is expressed at high levels (at protein
CC level) (PubMed:17420595). {ECO:0000269|PubMed:17420595,
CC ECO:0000305|PubMed:16810451}.
CC -!- DOMAIN: Has 3 domains, the helical N-terminus (residues 19-125), a
CC beta-barrel central domain (126-234) and a helical C-terminus (235-
CC 409). The C-terminus (410-417) forms part of the substrate-binding
CC pocket with the C-terminal helical domain (PubMed:24975806). The lid
CC loop assumes one of 2 conformations allowing opening and closing of the
CC active site (By similarity). {ECO:0000250|UniProtKB:A0A0C6DRW4,
CC ECO:0000269|PubMed:24975806}.
CC -!- BIOTECHNOLOGY: Expression in B.subtilis confers the ability to remove
CC sulfur from polycyclic aromatic sulfur compounds found in gasoline and
CC diesel (biodesulfurization), which are a considerable source of
CC pollution (PubMed:16810451). Modification of the operon so the start
CC codon of dszB no longer overlaps with the stop codon of dszA leads to
CC increased expression of DszB (in R.erythropolis) and about 5-fold
CC higher levels of desulfurization of DBT (PubMed:17420595).
CC Rearrangement of the operon into the order dszB-dszC-dszA leads to 12-
CC fold higher levels of DBT desulfurization (PubMed:18165370).
CC {ECO:0000269|PubMed:16810451, ECO:0000269|PubMed:17420595,
CC ECO:0000269|PubMed:18165370}.
CC -!- SIMILARITY: Belongs to the DszC flavin monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; DQ444325; ABE26646.1; -; Genomic_DNA.
DR PDB; 4JEK; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-417.
DR PDB; 4NXL; X-ray; 2.30 A; A/B/C/D=1-417.
DR PDBsum; 4JEK; -.
DR PDBsum; 4NXL; -.
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_0000455398"
FT REGION 19..125
FT /note="Helical N-terminus"
FT /evidence="ECO:0000269|PubMed:24975806"
FT REGION 126..234
FT /note="Central beta-barrel N-terminus"
FT /evidence="ECO:0000269|PubMed:24975806"
FT REGION 131..142
FT /note="Lid loop"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT REGION 235..409
FT /note="Helical C-terminus"
FT /evidence="ECO:0000269|PubMed:24975806"
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 96
FT /note="Y->A: Nearly wild-type catalytic activity."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 129
FT /note="N->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 161
FT /note="F->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 163
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 205
FT /note="W->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 215
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 250
FT /note="F->A,R: Near to total loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 338
FT /note="R->A: Loss of catalytic activity, does not form
FT tetramers."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 391
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 410..417
FT /note="Missing: Loss of catalytic activity, does not form
FT tetramers."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 415
FT /note="F->A: Decreased catalytic activity, still forms
FT tetramers."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 416
FT /note="T->A: Decreased catalytic activity, still forms
FT tetramers."
FT /evidence="ECO:0000269|PubMed:24975806"
FT MUTAGEN 417
FT /note="S->A: Nearly wild-type catalytic activity, still
FT forms tetramers."
FT /evidence="ECO:0000269|PubMed:24975806"
SQ SEQUENCE 417 AA; 45044 MW; 185DEBA927E74425 CRC64;
MTLSPEKEHV RPRDAADNDP VAVARGLAEK WRATAVERDR AGGSATAERE DLRASALLSL
LVPREYGGWG ADWPTAIEVV REIAAADGSL GHLFGYHLTN APMIELIGSQ EQEEHLYTQI
AQNNWWTGNA SSENNSHELD VKVSATPTED GGYVLNGTKH FCSGAKGSDL LFVFGVVQDD
SPQQGAIIAA AIPTSRAGVT PNDDWAAIGM RQTDSGSTDF HNVKVEPDEV LGAPNAFVLA
FIQSERGSLF RPIAQLIFAN VYLGIAHGAL DAAREYTRTQ ARPWTPAGIQ QATEDPYTIR
SYGEFTIALQ GADAAAREAA HLVQTVWDKG DALTPEDRGE LMAKVSGVKS LATNAALNIS
SGVFEVIGAR GTHPRYGFDR FWRNVRTHSL HDPVSYKIAD VGKHTLNGQY PIPGFTS
