ID   DSZD_RHOSH              Reviewed;         192 AA.
AC   Q6Q0M6;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=NADH:FMN oxidoreductase;
DE            EC=1.5.1.42 {ECO:0000250|UniProtKB:O68503, ECO:0000305|PubMed:16820450};
DE   AltName: Full=FMN reductase;
GN   Name=dszD {ECO:0000303|PubMed:16820450};
OS   Rhodococcus erythropolis (strain XP).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=1078016;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE FUNCTION, PATHWAY, AND
RP   BIOTECHNOLOGY.
RC   STRAIN=XP;
RX   PubMed=16820450; DOI=10.1128/aem.00081-06;
RA   Tao F., Yu B., Xu P., Ma C.Q.;
RT   "Biodesulfurization in biphasic systems containing organic solvents.";
RL   Appl. Environ. Microbiol. 72:4604-4609(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:16820450}.
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, ECO:0000305|PubMed:16820450};
CC   -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC       {ECO:0000269|PubMed:16820450}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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. As the substrates are not
CC       very soluble in conventional media, biphasic systems may help improve
CC       catalysis. Expression of dszD-dszA-dszB-dszC (cloned in this order) in
CC       organic-solvent-tolerant P.putida strain Idaho allows P.putida to grow
CC       on 10% p-xylene with DBT as the sole sulfur source. In this P.putida
CC       strain 97% of DBT was degraded, 71% of 4,6-dimethyldibenzothiophene and
CC       about 50% of 3-methyldibenzothiophene or 4-methyldibenzothiophene was
CC       degraded in the presence of 10% p-xylene. Degradation of DBT in the
CC       presence of 10% of other organic solvents was tested; when grown in
CC       dodecane, cyclohexane or heptanol bacteria metabolized DBT as well as
CC       p-xylene, while other organic solvents degraded DBT slightly less well.
CC       {ECO:0000269|PubMed:16820450}.
CC   -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase 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; AY569038; AAS77584.1; -; Genomic_DNA.
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; Flavoprotein; FMN; Nucleotide-binding; Oxidoreductase.
FT   CHAIN           1..192
FT                   /note="NADH:FMN oxidoreductase"
FT                   /id="PRO_0000455403"
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"
SQ   SEQUENCE   192 AA;  20435 MW;  C10D1C2C82C39A04 CRC64;
     MSDKPNAVSS HTTPDVPEVA ATPELSTGIC AGDYRAALRR HPAGVTVVTL DSGTGPVGFT
     ATSFSSVSLE PPLVSFNIAE TSSSINALKA AESLVIHLLG EHQQRLAQRF AGSADQRFAD
     ESLWAVLDTG EPVLHGTPSW MRVKVDQLIP VGDHTLVIGL VTRVHAEEDD ESAAAPLLYH
     EGKYYRPTPL GQ