ID   DSZD_RHOER              Reviewed;         192 AA.
AC   P0DW80;
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=NADH:FMN oxidoreductase;
DE            EC=1.5.1.42 {ECO:0000250|UniProtKB:O68503, ECO:0000305|PubMed:16810451};
DE   AltName: Full=FMN reductase;
GN   Name=dszD {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).
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. Provides
CC       DszA and DszC (DBTO2-monooxygenase and DBT-monooxygenase respectively)
CC       with reduced flavin (FMN). {ECO:0000250|UniProtKB:O68503,
CC       ECO:0000305|PubMed:16810451}.
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:0000250|UniProtKB:O68503};
CC   -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC       {ECO:0000269|PubMed:16810451}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Repressed by HBP or sulfate. {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. {ECO:0000269|PubMed:16810451}.
CC   -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ444326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   UniPathway; UPA00346; -.
PE   1: Evidence at protein level;
KW   Cytoplasm; Flavoprotein; FMN; Nucleotide-binding; Oxidoreductase.
FT   CHAIN           1..192
FT                   /note="NADH:FMN oxidoreductase"
FT                   /id="PRO_0000455402"
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"
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