ID   DSZB_RHOSH              Reviewed;         365 AA.
AC   Q6WNP2;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=2'-hydroxybiphenyl-2-sulfinate desulfinase {ECO:0000305};
DE            EC=3.13.1.3 {ECO:0000250|UniProtKB:P54997, ECO:0000305|PubMed:16820450};
DE   AltName: Full=2-(2-hydroxyphenyl)benzenesulfinate desulfinase {ECO:0000305};
DE            Short=HPBS desulfinase {ECO:0000305};
DE   AltName: Full=Dibenzothiophene desulfurization enzyme B {ECO:0000303|PubMed:16820450};
GN   Name=dszB {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 third and final step of the '4S'
CC       desulfurization pathway that removes covalently bound sulfur from
CC       dibenzothiophene (DBT) without breaking carbon-carbon bonds. Oxidizes
CC       2-(2'-hydroxyphenyl)benzene sulphinate (HBPS) to 2-hydroxybiphenyl
CC       (HBP) plus sulfite. The rate-limiting step of the '4S' desulfurization
CC       pathway. {ECO:0000250|UniProtKB:P54997, ECO:0000305|PubMed:16820450}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-hydroxybiphenyl-2-sulfinate + H2O = biphenyl-2-ol + H(+) +
CC         sulfite; Xref=Rhea:RHEA:12945, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17043, ChEBI:CHEBI:17359, ChEBI:CHEBI:18218; EC=3.13.1.3;
CC         Evidence={ECO:0000250|UniProtKB:P54997, ECO:0000305|PubMed:16820450};
CC   -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC       {ECO:0000269|PubMed:16820450}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P54997}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54997}.
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 DszB desulfinase family. {ECO:0000305}.
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DR   EMBL; AY278323; AAP33511.1; -; Genomic_DNA.
DR   SMR; Q6WNP2; -.
DR   UniPathway; UPA00346; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0018896; P:dibenzothiophene catabolic process; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..365
FT                   /note="2'-hydroxybiphenyl-2-sulfinate desulfinase"
FT                   /id="PRO_0000455395"
FT   ACT_SITE        27
FT                   /evidence="ECO:0000250|UniProtKB:P54997"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000250|UniProtKB:P54997"
FT   BINDING         27
FT                   /ligand="2'-hydroxybiphenyl-2-sulfinate"
FT                   /ligand_id="ChEBI:CHEBI:18218"
FT                   /evidence="ECO:0000250|UniProtKB:P54997"
FT   BINDING         60
FT                   /ligand="2'-hydroxybiphenyl-2-sulfinate"
FT                   /ligand_id="ChEBI:CHEBI:18218"
FT                   /evidence="ECO:0000250|UniProtKB:P54997"
FT   BINDING         70
FT                   /ligand="2'-hydroxybiphenyl-2-sulfinate"
FT                   /ligand_id="ChEBI:CHEBI:18218"
FT                   /evidence="ECO:0000250|UniProtKB:P54997"
FT   SITE            60
FT                   /note="May orient the sulfinate group"
FT                   /evidence="ECO:0000250|UniProtKB:P54997"
SQ   SEQUENCE   365 AA;  39045 MW;  DA6A867756DA23D6 CRC64;
     MTSRVDPANP GSELDSAIRD TLTYSNCPVP NALLTASESG FLDAAGIELD VLSGQQGTVH
     FTYDQPAYTR FGGEIPPLLS EGLRAPGRTR LLGITPLLGR QGFFVRDDSP ITAAADLAGR
     RIGVSASAIR ILRGQLGDYL ELDPWRQTLV ALGSWEARAL LHTLEHGELG VDDVELVPIS
     SPGVDVPAEQ LEESATVKGA DLFPDVARGQ AAVLASGDVD ALYSWLPWAG ELQATGARPV
     VDLGLDERNA YASVWTVSSG LVRQRPGLVQ RLVDAAVDAG LWARDHSDAV TSLHAANLGV
     STGAVGQGFG ADFQQRLVPR LDHDALALLE RTQQFLLTNN LLQEPVALDQ WAAPEFLNNS
     LNRHR