DSZD_RHOSG
ID DSZD_RHOSG Reviewed; 192 AA.
AC O68503;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=NADH:FMN oxidoreductase {ECO:0000303|PubMed:9634856};
DE EC=1.5.1.42 {ECO:0000269|PubMed:9634856};
DE AltName: Full=FMN reductase {ECO:0000303|PubMed:9634856};
DE AltName: Full=Flavin reductase {ECO:0000303|PubMed:9634856};
GN Name=dszD {ECO:0000303|PubMed:9634856};
OS Rhodococcus sp. (strain ATCC 53968 / IGTS8).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=54064;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 53968 / IGTS8;
RA Childs J.D., Li M.Z., Mitchell K., Emanule J., Gray K.A., Squires C.H.;
RT "Cloning of the dszD gene, encoding the NADH-FMN oxidoreductase required
RT for the activity of the dibenzothiophene and dibenzothiophene-sulfone
RT monooxygenases of Rhodococcus erythropolis strain IGTS8.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-41, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY, AND MUTAGENESIS OF THR-62.
RC STRAIN=ATCC 53968 / IGTS8;
RX PubMed=20349330; DOI=10.1007/s10529-010-0254-4;
RA Kamali N., Tavallaie M., Bambai B., Karkhane A.A., Miri M.;
RT "Site-directed mutagenesis enhances the activity of NADH-FMN oxidoreductase
RT (DszD) activity of Rhodococcus erythropolis.";
RL Biotechnol. Lett. 32:921-927(2010).
CC -!- FUNCTION: An NADH:FMN oxidoreductase which supplies reduced FMN for the
CC '4S' desulfurization pathway that removes covalently bound sulfur from
CC dibenzothiophene (DBT) without breaking carbon-carbon bonds
CC (PubMed:9634856, PubMed:20349330). Provides DszA and DszC (DBTO2-
CC monooxygenase and DBT-monooxygenase respectively) with reduced flavin
CC (FMN); has no activity on NADPH or FAD (PubMed:9634856). 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:20349330,
CC ECO:0000269|PubMed:9634856}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58210; EC=1.5.1.42;
CC Evidence={ECO:0000269|PubMed:20349330, ECO:0000269|PubMed:9634856};
CC -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC {ECO:0000269|PubMed:11823208, ECO:0000269|PubMed:9634856}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- BIOTECHNOLOGY: In association with the dszA-dszB-dsz operon can be used
CC to remove sulfur from polycyclic aromatic sulfur compounds found in
CC gasoline and diesel (biodesulfurization), which are a considerable
CC source of pollution. In addition it may be possible to engineer the
CC operon to make specialty chemicals (PubMed:11823208). Can be engineered
CC to make it more active, suggesting it may be possible increase the
CC yield and rate of the biodesulfurization process (PubMed:20349330).
CC {ECO:0000269|PubMed:11823208, ECO:0000269|PubMed:20349330}.
CC -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC {ECO:0000305}.
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DR EMBL; AF048979; AAC38226.1; -; Genomic_DNA.
DR SMR; O68503; -.
DR BioCyc; MetaCyc:MON-20854; -.
DR UniPathway; UPA00346; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016646; F:oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0018896; P:dibenzothiophene catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.30.110.10; -; 1.
DR InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Flavoprotein; FMN;
KW Nucleotide-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9634856"
FT CHAIN 2..192
FT /note="NADH:FMN oxidoreductase"
FT /id="PRO_0000455401"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60..63
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:B6CDL6"
FT BINDING 77..84
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:B6CDL6"
FT BINDING 111
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:B6CDL6"
FT BINDING 117
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:B6CDL6"
FT MUTAGEN 62
FT /note="T->A: Flavin reductase activity increases 7-fold."
FT /evidence="ECO:0000269|PubMed:20349330"
FT MUTAGEN 62
FT /note="T->N: Flavin reductase activity increases 5-fold."
FT /evidence="ECO:0000269|PubMed:20349330"
SQ SEQUENCE 192 AA; 20515 MW; 600C0C3D83C82A14 CRC64;
MSDKPNAVSS HTTPDVPEVA ATPELSTGIC AGDYRAALRR HPAGVTVVTL DSGTGPVGFT
ATSFSSVSLE PPLVSFNIAE TSSSINALKA AESLVIHLLG EHQQHLAQRF ARSADQRFAD
ESLWAVLDTG EPVLHGTPSW MRVKVDQLIP VGDHTLVIGL VTRVHAEEDD ESAAAPLLYH
EGKYYRPTPL GQ
