ID   NFSA_SALTY              Reviewed;         240 AA.
AC   Q9Z5Z2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Oxygen-insensitive NADPH nitroreductase {ECO:0000250|UniProtKB:P17117};
DE            EC=1.-.-.- {ECO:0000250|UniProtKB:P17117};
GN   Name=nfsA; Synonyms=mdaA, snrA; OrderedLocusNames=STM0874;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29629 / TA 1535;
RA   Lambert I.B., Boroumandi S., Nokhbeh M.R., Pokorny N.S., Koziarz P.;
RT   "Cloning and characterization of the major nitrotreductase from Salmonella
RT   typhimurium TA1535.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Catalyzes the reduction of nitroaromatic compounds using
CC       NADPH. Has a broad electron acceptor specificity. Reduces nitrofurazone
CC       by a ping-pong bi-bi mechanism possibly to generate a two-electron
CC       transfer product. {ECO:0000250|UniProtKB:P17117}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P17117};
CC       Note=Binds 1 FMN per monomer. {ECO:0000250|UniProtKB:P17117};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P17117}.
CC   -!- SIMILARITY: Belongs to the flavin oxidoreductase frp family.
CC       {ECO:0000305}.
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DR   EMBL; AF117952; AAD18027.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19810.1; -; Genomic_DNA.
DR   RefSeq; NP_459851.1; NC_003197.2.
DR   RefSeq; WP_000075300.1; NC_003197.2.
DR   AlphaFoldDB; Q9Z5Z2; -.
DR   SMR; Q9Z5Z2; -.
DR   STRING; 99287.STM0874; -.
DR   PaxDb; Q9Z5Z2; -.
DR   EnsemblBacteria; AAL19810; AAL19810; STM0874.
DR   GeneID; 1252393; -.
DR   KEGG; stm:STM0874; -.
DR   PATRIC; fig|99287.12.peg.913; -.
DR   HOGENOM; CLU_070764_0_2_6; -.
DR   OMA; GMCLGYP; -.
DR   PhylomeDB; Q9Z5Z2; -.
DR   BioCyc; SENT99287:STM0874-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02146; NfsA-like; 1.
DR   Gene3D; 3.40.109.10; -; 1.
DR   InterPro; IPR016446; Flavin_OxRdtase_Frp.
DR   InterPro; IPR029479; Nitroreductase.
DR   InterPro; IPR000415; Nitroreductase-like.
DR   PANTHER; PTHR43425; PTHR43425; 1.
DR   Pfam; PF00881; Nitroreductase; 1.
DR   PIRSF; PIRSF005426; Frp; 1.
DR   SUPFAM; SSF55469; SSF55469; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..240
FT                   /note="Oxygen-insensitive NADPH nitroreductase"
FT                   /id="PRO_0000205511"
FT   BINDING         11..15
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P17117"
FT   BINDING         39
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P17117"
FT   BINDING         67
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P17117"
FT   BINDING         128..131
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P17117"
FT   BINDING         167..169
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P17117"
FT   CONFLICT        24..25
FT                   /note="DA -> EP (in Ref. 1; AAD18027)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31..33
FT                   /note="IAA -> NCR (in Ref. 1; AAD18027)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61..62
FT                   /note="VP -> SC (in Ref. 1; AAD18027)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="D -> G (in Ref. 1; AAD18027)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   240 AA;  26926 MW;  8E615E7ABDA44D84 CRC64;
     MSPTIELLCG HRSIRHFTDE PVTDAQREAI IAAARSTSSS SFLQCSSIIR ITDRALREAL
     VPLTGGQKHV AQAAEFWVFC ADFNRHLQIC PDAQLGLAEQ LLLGVVDTAM MGQNALTAAE
     SLGLGGVYIG GIRNNIESVT ELLKLPKHVL PLFGLCLGWP ADNPDLKPRL PAELVVHENQ
     YQPLDEKLLA RYDEQLAEYY LTRGSNTRRD TWSDHIRRTL IKENRPFILE YLHKQGWATR