DSZA_RHOER
ID DSZA_RHOER Reviewed; 453 AA.
AC Q0ZIH7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Dibenzothiophene-sulfone monooxygenase;
DE Short=DBTO2 monooxygenase;
DE Short=DBTO2-MO;
DE EC=1.14.14.22 {ECO:0000250|UniProtKB:P54995, ECO:0000305|PubMed:16810451};
GN Name=dszA {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).
CC -!- FUNCTION: Catalyzes the second step of the '4S' desulfurization pathway
CC that removes covalently bound sulfur from dibenzothiophene (DBT)
CC without breaking carbon-carbon bonds. Metabolizes DBT-sulfone (DBTO2 or
CC DBT 5,5-dioxide) to 2-(2'-hydroxyphenyl)benzene sulphinate (HBPS).
CC {ECO:0000250|UniProtKB:P54995, ECO:0000305|PubMed:16810451}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dibenzothiophene 5,5-dioxide + FMNH2 + NADH + O2 = 2'-
CC hydroxybiphenyl-2-sulfinate + FMN + H(+) + H2O + NAD(+);
CC Xref=Rhea:RHEA:12312, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:18218, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:57945, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:90356; EC=1.14.14.22;
CC Evidence={ECO:0000250|UniProtKB:P54995, ECO:0000305|PubMed:16810451};
CC -!- COFACTOR:
CC Note=Reduced flavin is provided by flavin reductase DszD.
CC {ECO:0000250|UniProtKB:P54995};
CC -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC {ECO:0000269|PubMed:16810451}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P54995}.
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 -!- 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 NtaA/SnaA/DszA monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; DQ444325; ABE26644.1; -; Genomic_DNA.
DR UniPathway; UPA00346; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0018896; P:dibenzothiophene catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01095; Nitrilotriacetate_monoxgenase; 1.
DR Gene3D; 3.20.20.30; -; 1.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR016215; NTA_MOA.
DR Pfam; PF00296; Bac_luciferase; 1.
DR PIRSF; PIRSF000337; NTA_MOA; 1.
DR SUPFAM; SSF51679; SSF51679; 1.
DR TIGRFAMs; TIGR03860; FMN_nitrolo; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Flavoprotein; FMN; Monooxygenase; Nucleotide-binding;
KW Oxidoreductase.
FT CHAIN 1..453
FT /note="Dibenzothiophene-sulfone monooxygenase"
FT /id="PRO_0000455392"
FT BINDING 59
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
FT BINDING 156..160
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
FT BINDING 228..231
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
SQ SEQUENCE 453 AA; 49612 MW; 85BC9494251AA7C3 CRC64;
MTQQRQMDLA GFFSAGNVTH AHGAWRHTDA SNDFLSGKYY QHIARTLERG KFDLLFLPDG
LAVEDSYGDN LDTGVGLGGQ GAVALEPASV VATMAAVTEH LGLGATISAT YYPPYHVARV
FATLDQLSGG RVSWNVVTSL NDAEARNFGI NQHLEHDARY DRADEFLEAV KKLWNSWDED
ALVLDKAAGV FADPAKVHYV DHHGEWLNVR GPLQVPRSPQ GEPVILQAGL SPRGRRFAGK
WAEAVFSLAP NLEVMQATYQ GIKAEVDAAG RDPDQTKIFT AVMPVLGESQ AVAQERLEYL
NSLVHPEVGL STLSSHTGIN LAAYPLDTPI KDILRDLQDR NVPTQLHMFA AATHSEELTL
AEMGRRYGTN VGFVPQWAGT GEQIADELIR HFEGGAADGF IISPAFLPGS YDEFVDQVVP
VLQDRGYFRT EYQGNTLRDH LGLRVPQLQG QPS
