DSZA_RHOSG
ID DSZA_RHOSG Reviewed; 453 AA.
AC P54995;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Dibenzothiophene-sulfone monooxygenase;
DE Short=DBTO2 monooxygenase {ECO:0000303|PubMed:9634856};
DE Short=DBTO2-MO {ECO:0000303|PubMed:9634856};
DE EC=1.14.14.22 {ECO:0000269|PubMed:9634856};
DE AltName: Full=Dibenzothiophene desulfurization enzyme A;
GN Name=dszA {ECO:0000303|PubMed:7574582};
GN Synonyms=soxA {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, PATHWAY, PROBABLE OPERON
RP 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, DISRUPTION PHENOTYPE, 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, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND 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, 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 [6]
RP FUNCTION, PATHWAY, AND MUTAGENESIS OF GLN-345.
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).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF THR-344; GLN-345 AND LEU-346.
RC STRAIN=ATCC 53968 / IGTS8;
RX PubMed=12967013; DOI=10.1023/a:1024564430107;
RA Konishi J., Maruhashi K.;
RT "Residue 345 of dibenzothiophene (DBT) sulfone monooxygenase is involved in
RT C-S bond cleavage specificity of alkylated DBT sulfones.";
RL Biotechnol. Lett. 25:1199-1202(2003).
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 an unidentified intermediate (not 2-hydroxybiphenyl
CC (2-HBP)). DszA and DszB together metabolize DBTO2 to 2-HBP
CC (PubMed:7961424, PubMed:7574582). Metabolizes DBTO2 to 2-(2'-
CC hydroxyphenyl)benzene sulphinate (HBPS), also converts BPSo
CC (biphenylenesultone (dibenz[c,e][l,2]oxathiin-6,6-dioxide)) to DHBP
CC (2,2'-dihydroxybiphenyl) and sulfite (PubMed:9308179). The pathway
CC substrate specificity has been augmented using mutagenesis, however no
CC mutations allowed use of alkylated thiophenes (PubMed:11823208). Also
CC acts on 3-methyl DBT sulfone (3-methyl dibenzothiophene 5,5-dioxide)
CC yielding the 3-methylated derivative; mutating Gln-345 alters the
CC product isomer ratio (PubMed:12967013). {ECO:0000269|PubMed:11823208,
CC ECO:0000269|PubMed:12967013, ECO:0000269|PubMed:7574582,
CC ECO:0000269|PubMed:7961424, ECO:0000269|PubMed:9308179}.
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:0000269|PubMed:9634856};
CC -!- COFACTOR:
CC Note=Reduced flavin is provided by flavin reductase DszD.
CC {ECO:0000269|PubMed:9634856};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for dibenzothiophene 5,5-dioxide
CC {ECO:0000269|PubMed:9634856};
CC Note=kcat is about 1 sec(-1). {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: Homodimer. {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 -!- DISRUPTION PHENOTYPE: DBTO2 but not 2-HBP is detected following growth
CC on DBT. {ECO:0000269|PubMed:7574582, 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 NtaA/SnaA/DszA monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; U08850; AAA56671.1; -; Genomic_DNA.
DR EMBL; L37363; AAA99482.1; -; Genomic_DNA.
DR AlphaFoldDB; P54995; -.
DR SMR; P54995; -.
DR KEGG; ag:AAA99482; -.
DR BioCyc; MetaCyc:MON-265; -.
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; Plasmid.
FT CHAIN 1..453
FT /note="Dibenzothiophene-sulfone monooxygenase"
FT /id="PRO_0000072043"
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"
FT MUTAGEN 344
FT /note="T->A: No change in product isomers on 3-methyl DBT
FT sulfone."
FT /evidence="ECO:0000269|PubMed:12967013"
FT MUTAGEN 345
FT /note="Q->A: In dszA1; strain can also use octyl sulfide.
FT Alters the product isomer ratio on 3-methyl DBT sulfone."
FT /evidence="ECO:0000269|PubMed:11823208,
FT ECO:0000269|PubMed:12967013"
FT MUTAGEN 346
FT /note="L->A: No change in product isomers on 3-methyl DBT
FT sulfone."
FT /evidence="ECO:0000269|PubMed:12967013"
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
