DSZA_RHOSH
ID DSZA_RHOSH Reviewed; 453 AA.
AC Q6WNP3;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
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:16820450};
DE AltName: Full=Dibenzothiophene desulfurization enzyme A {ECO:0000303|PubMed:16820450};
GN Name=dszA {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).
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:16820450}.
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:16820450};
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:16820450}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P54995}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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 NtaA/SnaA/DszA monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AY278323; AAP33509.1; -; Genomic_DNA.
DR SMR; Q6WNP3; -.
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_0000455393"
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; 49635 MW; 3A45E2D097259C82 CRC64;
MTQQRQMHLA 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
