NFSB_SALTY
ID NFSB_SALTY Reviewed; 217 AA.
AC P15888;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Oxygen-insensitive NAD(P)H nitroreductase;
DE EC=1.-.-.-;
GN Name=nfsB {ECO:0000250|UniProtKB:P38489};
GN Synonyms=nfnB {ECO:0000312|EMBL:AAL19529.1}, nfsI;
GN OrderedLocusNames=STM0578;
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 29631 / TA 1538;
RX PubMed=2179862; DOI=10.1093/nar/18.4.1059;
RA Watanabe M., Ishidate M., Nohmi T.;
RT "Nucleotide sequence of Salmonella typhimurium nitroreductase gene.";
RL Nucleic Acids Res. 18:1059-1059(1990).
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: Reduction of a variety of nitroaromatic compounds using NADH
CC (and to lesser extent NADPH) as source of reducing equivalents; two
CC electrons are transferred. Capable of reducing nitrofurazone (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; X17250; CAA35113.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19529.1; -; Genomic_DNA.
DR PIR; S08397; S08397.
DR RefSeq; NP_459570.1; NC_003197.2.
DR RefSeq; WP_000355879.1; NC_003197.2.
DR PDB; 3HZN; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-217.
DR PDBsum; 3HZN; -.
DR AlphaFoldDB; P15888; -.
DR SMR; P15888; -.
DR STRING; 99287.STM0578; -.
DR PaxDb; P15888; -.
DR EnsemblBacteria; AAL19529; AAL19529; STM0578.
DR GeneID; 1252098; -.
DR KEGG; stm:STM0578; -.
DR PATRIC; fig|99287.12.peg.610; -.
DR HOGENOM; CLU_070764_4_1_6; -.
DR OMA; PWHFVVA; -.
DR PhylomeDB; P15888; -.
DR BioCyc; SENT99287:STM0578-MON; -.
DR BRENDA; 1.7.1.16; 5542.
DR EvolutionaryTrace; P15888; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0018545; F:NAD(P)H nitroreductase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046256; P:2,4,6-trinitrotoluene catabolic process; IBA:GO_Central.
DR CDD; cd02149; NfsB-like; 1.
DR Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR033878; NfsB-like.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..217
FT /note="Oxygen-insensitive NAD(P)H nitroreductase"
FT /id="PRO_0000072713"
FT BINDING 10..14
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q01234"
FT BINDING 41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q01234"
FT BINDING 71
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q01234"
FT BINDING 74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q01234"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q01234"
FT BINDING 165..166
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 205..207
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3HZN"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:3HZN"
FT STRAND 78..89
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 111..129
FT /evidence="ECO:0007829|PDB:3HZN"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 135..156
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:3HZN"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3HZN"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:3HZN"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3HZN"
SQ SEQUENCE 217 AA; 23955 MW; E90E9E05A0826D0F CRC64;
MDIVSVALQR YSTKAFDPSK KLTAEEADKI KTLLQYSPSS TNSQPWHFIV ASTEEGKARV
AKSAAGNYTF NERKMLDASH VVVFCAKTAM DDAWLERVVD QEDADGRFAT PEAKAANDKG
RRFFADMHRV SLKDDHQWMA KQVYLNVGNF LLGVAAMGLD AVPIEGFDAE VLDAEFGLKE
KGYTSLVVVP VGHHSVEDFN AGLPKSRLPL ETTLTEV
