DSZC_MYCGD
ID DSZC_MYCGD Reviewed; 415 AA.
AC B2CML6; G1C5K8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Dibenzothiophene monooxygenase {ECO:0000303|PubMed:19144512};
DE Short=DBT monooxygenase;
DE Short=DBT-MO;
DE EC=1.14.14.21 {ECO:0000269|PubMed:19144512};
GN Name=dszC {ECO:0000303|PubMed:19144512};
OS Mycobacterium goodii (Mycolicibacterium goodii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=134601;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, AND PATHWAY.
RC STRAIN=X7B;
RX PubMed=19144512; DOI=10.1016/j.biortech.2008.12.009;
RA Li J., Feng J., Li Q., Ma C., Yu B., Gao C., Wu G., Xu P.;
RT "Both FMNH2 and FADH2 can be utilized by the dibenzothiophene monooxygenase
RT from a desulfurizing bacterium Mycobacterium goodii X7B.";
RL Bioresour. Technol. 100:2594-2599(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X7B {ECO:0000312|EMBL:AEK97796.1};
RA Li Q., Su F., Tao F., Ma C., Xu P.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X7B;
RX PubMed=26278197; DOI=10.1016/j.jbiotec.2015.08.004;
RA Yu B., Tao F., Li F., Hou J., Tang H., Ma C., Xu P.;
RT "Complete genome sequence of Mycobacterium goodii X7B, a facultative
RT thermophilic biodesulfurizing bacterium with industrial potential.";
RL J. Biotechnol. 212:56-57(2015).
CC -!- FUNCTION: Catalyzes the first step of the '4S' desulfurization pathway
CC that removes covalently bound sulfur from dibenzothiophene (DBT)
CC without breaking carbon-carbon bonds. Sulfur dioxygenase which converts
CC DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) probably in a stepwise
CC manner. In addition to FMNH2 can also use FAD (although FAD is less
CC efficient). {ECO:0000269|PubMed:19144512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dibenzothiophene + 2 FMNH2 + 2 O2 = dibenzothiophene 5,5-
CC dioxide + 2 FMN + 2 H(+) + 2 H2O; Xref=Rhea:RHEA:49072,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:23681, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:90356; EC=1.14.14.21;
CC Evidence={ECO:0000269|PubMed:19144512};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dibenzothiophene + FMNH2 + O2 = dibenzothiophene 5-oxide + FMN
CC + H(+) + H2O; Xref=Rhea:RHEA:49076, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23681,
CC ChEBI:CHEBI:23683, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000305|PubMed:19144512};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dibenzothiophene 5-oxide + FMNH2 + O2 = dibenzothiophene 5,5-
CC dioxide + FMN + H(+) + H2O; Xref=Rhea:RHEA:49080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23683,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90356;
CC Evidence={ECO:0000305|PubMed:19144512};
CC -!- COFACTOR:
CC Note=Reduced flavin is provided by flavin reductase DszD; in a coupled
CC DszC-DszD reaction both FMNH2 and FADH2 can be used, maximal DBTO2
CC production is seen with 5 uM FMN or with 35 uM FAD.
CC {ECO:0000269|PubMed:19144512};
CC -!- ACTIVITY REGULATION: Inhibited at high concentrations of FMN or FAD.
CC {ECO:0000269|PubMed:19144512}.
CC -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC {ECO:0000305|PubMed:19144512}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q0ZIH5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The lid loop assumes one of 2 conformations allowing opening
CC and closing of the active site. {ECO:0000250|UniProtKB:A0A0C6DRW4}.
CC -!- SIMILARITY: Belongs to the DszC flavin monooxygenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU527978; ACB32256.1; -; Genomic_DNA.
DR EMBL; JF740062; AEK97796.1; -; Genomic_DNA.
DR EMBL; CP012150; AKS33209.1; -; Genomic_DNA.
DR STRING; 134601.AFA91_16295; -.
DR EnsemblBacteria; AKS33209; AKS33209; AFA91_16295.
DR KEGG; mgo:AFA91_16295; -.
DR PATRIC; fig|134601.6.peg.3381; -.
DR OrthoDB; 760677at2; -.
DR BRENDA; 1.14.14.21; 13503.
DR UniPathway; UPA00346; -.
DR Proteomes; UP000062255; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0018896; P:dibenzothiophene catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Flavoprotein; FMN; Monooxygenase; Nucleotide-binding;
KW Oxidoreductase.
FT CHAIN 1..415
FT /note="Dibenzothiophene monooxygenase"
FT /id="PRO_0000455396"
FT REGION 129..140
FT /note="Lid loop"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 94
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 127..132
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 157..161
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 280
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 365..366
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT BINDING 387
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0A0C6DRW4"
FT CONFLICT 4..38
FT /note="TDDTTTAQNSRHGDPIEVARELTRKWQTTVVERDK -> SPEKQHVRPRDAA
FT DNDPVAVARGLAEKWRATAVERDR (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="E -> A (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 58..69
FT /note="VTVPRHLGGWGA -> LLVPREYGGWGT (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="L -> I (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..84
FT /note="KV -> AA (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..120
FT /note="STPAVIDLWGSPEQKERLLRQLAE -> TNAPMIELIGSQEQEEHLYTQIAQ
FT (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="I -> V (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..160
FT /note="TATPADDGGYFFNGIKHFS -> SATPTEDGGYVLNGTKHFC (in Ref.
FT 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 170..179
FT /note="LVFGVIPEGF -> FVFGVVQDDS (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="V -> I (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 193..198
FT /note="TREGVQ -> SRAGVT (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..224
FT /note="QALGMRRTDSGTTEFHNVAVR -> AAIGMRQTDSGSTDFHNVKVE (in
FT Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 231..243
FT /note="KPNAILEAFLASG -> APNAFVLAFIQSE (in Ref. 1;
FT ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..258
FT /note="GPIVQLVFSS -> APIAQLIFAN (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 265..270
FT /note="RGALET -> HGALDA (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..291
FT /note="VTQAV -> IQQAT (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 304..309
FT /note="GIQLQA -> TIALQG (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..324
FT /note="QLLQAA -> HLLQTV (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 333..335
FT /note="SQE -> PED (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 342..343
FT /note="QI -> KV (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..361
FT /note="IATQAALDVTSRI -> LATNAALNISSGV (in Ref. 1;
FT ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="K -> R (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 383..387
FT /note="IRTHT -> VRTHS (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..407
FT /note="EVGNYVLNQR -> DVGKHTLNGQ (in Ref. 1; ACB32256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 45339 MW; 27575D5FC3E3AA93 CRC64;
MTLTDDTTTA QNSRHGDPIE VARELTRKWQ TTVVERDKAG GSATEEREDL RASGLLSVTV
PRHLGGWGAD WPTALEVVRE IAKVDGSLGH LFGYHLSTPA VIDLWGSPEQ KERLLRQLAE
NNWWTGNASS ENNSHILDWK VTATPADDGG YFFNGIKHFS SGAKGSDLLL VFGVIPEGFP
QQGAIVAAAI PTTREGVQPN DDWQALGMRR TDSGTTEFHN VAVRPDEVLG KPNAILEAFL
ASGRGSLFGP IVQLVFSSVY LGIARGALET AREYTRTQAR PWTPAGVTQA VEDPYTIRSY
GEFGIQLQAA DAAAREAAQL LQAAWDKGDA LTSQERGELM VQISGVKAIA TQAALDVTSR
IFEVIGARGT HPKYGFDRFW RNIRTHTLHD PVSYKIAEVG NYVLNQRYPI PGFTS
