ID   DSZD_MYCGD              Reviewed;         161 AA.
AC   B6CDL6;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=NADH:FMN oxidoreductase;
DE            EC=1.5.1.37 {ECO:0000269|PubMed:19144512};
DE            EC=1.5.1.42 {ECO:0000269|PubMed:19144512};
DE   AltName: Full=FAD reductase (NADH);
DE   AltName: Full=FMN reductase;
DE   AltName: Full=Flavin reductase {ECO:0000303|PubMed:19144512};
GN   Name=dszD {ECO:0000303|PubMed:19144512}; ORFNames=AFA91_09010;
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, AND
RP   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;
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).
RN   [3] {ECO:0007744|PDB:3PFT}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 5-161 IN COMPLEX WITH FMN.
RA   Li Q., Xu P., Ma C., Gu L., Liu X., Zhang C., Li N., Su J., Li B., Liu S.;
RT   "The flavin reductase DSZD from a desulfurizing mycobacterium goodii
RT   strain: systemic manipulation and investigation based on the crystal
RT   structure.";
RL   Submitted (OCT-2010) to the PDB data bank.
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. Can also
CC       use FAD. Provides DszC and probably also DszA (DBT-monooxygenase and
CC       DBTO2-monooxygenase respectively) with reduced flavin (FMN and/or FAD).
CC       {ECO:0000269|PubMed:19144512}.
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:19144512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FADH2 + NAD(+) = FAD + 2 H(+) + NADH; Xref=Rhea:RHEA:30147,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58307; EC=1.5.1.37;
CC         Evidence={ECO:0000269|PubMed:19144512};
CC   -!- PATHWAY: Sulfur metabolism; dibenzothiophene degradation.
CC       {ECO:0000305|PubMed:19144512}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC       {ECO:0000305}.
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DR   EMBL; EU154996; ABX11274.1; -; Genomic_DNA.
DR   EMBL; CP012150; AKS31988.1; -; Genomic_DNA.
DR   RefSeq; WP_049744407.1; NZ_CP012150.1.
DR   PDB; 3PFT; X-ray; 1.60 A; A/B=5-161.
DR   PDBsum; 3PFT; -.
DR   SMR; B6CDL6; -.
DR   STRING; 134601.AFA91_09010; -.
DR   EnsemblBacteria; AKS31988; AKS31988; AFA91_09010.
DR   KEGG; mgo:AFA91_09010; -.
DR   PATRIC; fig|134601.6.peg.1871; -.
DR   OrthoDB; 1681849at2; -.
DR   UniPathway; UPA00346; -.
DR   Proteomes; UP000062255; Chromosome.
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   3D-structure; Cytoplasm; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW   Oxidoreductase.
FT   CHAIN           1..161
FT                   /note="NADH:FMN oxidoreductase"
FT                   /id="PRO_0000455400"
FT   BINDING         30
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0007744|PDB:3PFT"
FT   BINDING         37..40
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0007744|PDB:3PFT"
FT   BINDING         54..61
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0007744|PDB:3PFT"
FT   BINDING         88
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0007744|PDB:3PFT"
FT   BINDING         94
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0007744|PDB:3PFT"
FT   BINDING         151
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0007744|PDB:3PFT"
SQ   SEQUENCE   161 AA;  16879 MW;  734572180F3A0FA8 CRC64;
     MSATDLSPTS LREAFGHFPS GVIAIAAEVD GTRVGLAAST FVPVSLEPPL VAFCVQNSST
     TWPKLKDLPS LGISVLGEAH DTAARTLAAK TGDRFAGLET ESRDSGAVFI NGTSVWLESA
     IEQLVPAGDH TIVVLRVSDI VINEAVPPIV FHRSAFRKLG A