DSZB_RHOSG
ID DSZB_RHOSG Reviewed; 365 AA.
AC P54997;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=2'-hydroxybiphenyl-2-sulfinate desulfinase {ECO:0000303|PubMed:31545606};
DE EC=3.13.1.3 {ECO:0000269|PubMed:9634856};
DE AltName: Full=2-(2-hydroxyphenyl)benzenesulfinate desulfinase {ECO:0000303|PubMed:9634856};
DE Short=HPBS desulfinase {ECO:0000303|PubMed:9634856};
DE AltName: Full=Dibenzothiophene desulfurization enzyme B {ECO:0000305};
GN Name=dszB {ECO:0000303|PubMed:7574582};
GN Synonyms=soxB {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], PATHWAY, PROBABLE OPERON STRUCTURE,
RP 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, 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, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP 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, PATHWAY, SUBCELLULAR LOCATION, 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 BIOTECHNOLOGY.
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, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 53968 / IGTS8;
RX PubMed=31545606; DOI=10.1021/acs.jpcb.9b05252;
RA Yu Y., Mills L.C., Englert D.L., Payne C.M.;
RT "Inhibition Mechanisms of Rhodococcus Erythropolis 2'-Hydroxybiphenyl-2-
RT sulfinate Desulfinase (DszB).";
RL J. Phys. Chem. B 123:9054-9065(2019).
RN [8] {ECO:0007744|PDB:2DE2, ECO:0007744|PDB:2DE3, ECO:0007744|PDB:2DE4}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) ALONE AND IN COMPLEX WITH SUBSTRATE,
RP SUBUNIT, ACTIVE SITES, DOMAIN, AND MUTAGENESIS OF CYS-27; HIS-60; ARG-70
RP AND GLU-192.
RC STRAIN=ATCC 53968 / IGTS8;
RX PubMed=16891315; DOI=10.1074/jbc.m602974200;
RA Lee W.C., Ohshiro T., Matsubara T., Izumi Y., Tanokura M.;
RT "Crystal structure and desulfurization mechanism of 2'-hydroxybiphenyl-2-
RT sulfinic acid desulfinase.";
RL J. Biol. Chem. 281:32534-32539(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 (PubMed:7961424, PubMed:7574582, PubMed:9634856,
CC PubMed:9308179, PubMed:31545606). The rate-limiting step of the '4S'
CC desulfurization pathway (PubMed:9308179, PubMed:31545606). The pathway
CC substrate specificity has been augmented using mutagenesis, however no
CC mutations allowed use of alkylated thiophenes (PubMed:11823208).
CC {ECO:0000269|PubMed:11823208, ECO:0000269|PubMed:31545606,
CC ECO:0000269|PubMed:7574582, ECO:0000269|PubMed:7961424,
CC ECO:0000269|PubMed:9308179, ECO:0000269|PubMed:9634856}.
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:0000269|PubMed:31545606, ECO:0000269|PubMed:9634856};
CC -!- ACTIVITY REGULATION: Inhibited by the end product HBP.
CC {ECO:0000269|PubMed:31545606}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 uM for HBPS {ECO:0000269|PubMed:31545606};
CC Note=kcat is 2 min(-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: Monomer. {ECO:0000269|PubMed:16891315,
CC ECO:0000269|PubMed:9634856}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9308179}.
CC -!- INDUCTION: Expressed during growth on DBT or DMSO as sole sulfur
CC source; this protein accumulates to lower levels than DszA or DszC (at
CC protein level) (PubMed:8932295). Part of the probable dszA-dszB-dszC
CC operon (Probable). Desulfurization is repressed by sulfate, cysteine
CC 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 -!- DOMAIN: Has 2 domains; domain A (residues 1-97 and 252-365) and domain
CC B (residues 98-251). The active site with bound substrates is found
CC between them. Upon substrate binding His-60 moves into the active site.
CC {ECO:0000269|PubMed:16891315}.
CC -!- DISRUPTION PHENOTYPE: Blocks the desulfurization of DBT to 2-HBP,
CC accumulates an unknown intermediate that is not DBTO2.
CC {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 DszB desulfinase family. {ECO:0000305}.
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DR EMBL; U08850; AAA56672.1; -; Genomic_DNA.
DR EMBL; L37363; AAA99483.1; -; Genomic_DNA.
DR PDB; 2DE2; X-ray; 1.80 A; A=1-365.
DR PDB; 2DE3; X-ray; 1.60 A; A/B=1-365.
DR PDB; 2DE4; X-ray; 1.80 A; A/B=1-365.
DR PDBsum; 2DE2; -.
DR PDBsum; 2DE3; -.
DR PDBsum; 2DE4; -.
DR AlphaFoldDB; P54997; -.
DR SMR; P54997; -.
DR DrugBank; DB07483; 1,1'-BIPHENYL-2-SULFINIC ACID.
DR DrugBank; DB08319; 2'-HYDROXY-1,1'-BIPHENYL-2-SULFINIC ACID.
DR KEGG; ag:AAA99483; -.
DR BioCyc; MetaCyc:MON-266; -.
DR BRENDA; 3.13.1.3; 5389.
DR UniPathway; UPA00346; -.
DR EvolutionaryTrace; P54997; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018740; F:2'-hydroxybiphenyl-2-sulfinate desulfinase activity; IEA:UniProtKB-EC.
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 3D-structure; Cytoplasm; Hydrolase; Monooxygenase; Oxidoreductase; Plasmid.
FT CHAIN 1..365
FT /note="2'-hydroxybiphenyl-2-sulfinate desulfinase"
FT /id="PRO_0000072047"
FT ACT_SITE 27
FT /evidence="ECO:0000305|PubMed:16891315"
FT ACT_SITE 70
FT /evidence="ECO:0000305|PubMed:16891315"
FT BINDING 27
FT /ligand="2'-hydroxybiphenyl-2-sulfinate"
FT /ligand_id="ChEBI:CHEBI:18218"
FT /evidence="ECO:0000269|PubMed:16891315,
FT ECO:0007744|PDB:2DE3, ECO:0007744|PDB:2DE4"
FT BINDING 60
FT /ligand="2'-hydroxybiphenyl-2-sulfinate"
FT /ligand_id="ChEBI:CHEBI:18218"
FT /evidence="ECO:0000269|PubMed:16891315,
FT ECO:0007744|PDB:2DE3, ECO:0007744|PDB:2DE4"
FT BINDING 70
FT /ligand="2'-hydroxybiphenyl-2-sulfinate"
FT /ligand_id="ChEBI:CHEBI:18218"
FT /evidence="ECO:0000269|PubMed:16891315,
FT ECO:0007744|PDB:2DE3, ECO:0007744|PDB:2DE4"
FT SITE 60
FT /note="May orient the sulfinate group"
FT /evidence="ECO:0000305|PubMed:16891315"
FT MUTAGEN 27
FT /note="C->S: Loss of desulfination activity."
FT /evidence="ECO:0000269|PubMed:16891315"
FT MUTAGEN 60
FT /note="H->Q: About 17-fold decrease in desulfination
FT activity."
FT /evidence="ECO:0000269|PubMed:16891315"
FT MUTAGEN 70
FT /note="R->I,K: Loss of desulfination activity, protein
FT found in insoluble cell extract."
FT /evidence="ECO:0000269|PubMed:16891315"
FT MUTAGEN 192
FT /note="E->Q: No change in desulfination activity."
FT /evidence="ECO:0000269|PubMed:16891315"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:2DE3"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:2DE3"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:2DE3"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:2DE3"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2DE3"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2DE3"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:2DE3"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:2DE3"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:2DE3"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2DE3"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:2DE3"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:2DE3"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 266..283
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 302..309
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 323..338
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:2DE3"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:2DE3"
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
