DSZB_RHOER
ID DSZB_RHOER Reviewed; 365 AA.
AC P0DW79;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 1.
DT 03-AUG-2022, entry version 1.
DE RecName: Full=2'-hydroxybiphenyl-2-sulfinate desulfinase {ECO:0000305};
DE EC=3.13.1.3 {ECO:0000250|UniProtKB:P54997, ECO:0000305|PubMed:16810451};
DE AltName: Full=2-(2-hydroxyphenyl)benzenesulfinate desulfinase {ECO:0000305|PubMed:16810451};
DE Short=HPBS desulfinase {ECO:0000305|PubMed:16810451};
GN Name=dszB {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 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:16810451}.
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:16810451};
CC -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC {ECO:0000269|PubMed:16810451}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P54997}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54997}.
CC -!- INDUCTION: Repressed by HBP or sulfate (Probable). Part of the dszA-
CC dszB-dszC operon. This protein is expressed at quite low levels in
CC R.erythropolis (at protein level) (PubMed:17420595).
CC {ECO:0000269|PubMed:17420595, 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 DszB desulfinase family. {ECO:0000305}.
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DR EMBL; DQ444325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR UniPathway; UPA00346; -.
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_0000455394"
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
