NFSB_ENTCL
ID NFSB_ENTCL Reviewed; 217 AA.
AC Q01234;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Oxygen-insensitive NAD(P)H nitroreductase;
DE Short=NR;
DE EC=1.-.-.-;
GN Name=nfsB {ECO:0000250|UniProtKB:P38489};
GN Synonyms=nfnB, nfsI {ECO:0000312|EMBL:AAA62801.1};
OS Enterobacter cloacae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43560 / 96-3;
RX PubMed=1999406; DOI=10.1016/s0021-9258(20)64295-8;
RA Bryant C., Hubbard L., McElroy W.D.;
RT "Cloning, nucleotide sequence, and expression of the nitroreductase gene
RT from Enterobacter cloacae.";
RL J. Biol. Chem. 266:4126-4130(1991).
RN [2]
RP CHARACTERIZATION.
RX PubMed=1999405; DOI=10.1016/s0021-9258(20)64294-6;
RA Bryant C., Deluca M.;
RT "Purification and characterization of an oxygen-insensitive NAD(P)H
RT nitroreductase from Enterobacter cloacae.";
RL J. Biol. Chem. 266:4119-4125(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH FMN; ACETATE AND
RP BENZOIC ACID, AND SUBUNIT.
RX PubMed=11805110; DOI=10.1074/jbc.m111334200;
RA Haynes C.A., Koder R.L., Miller A.-F., Rodgers D.W.;
RT "Structures of nitroreductase in three states: effects of inhibitor binding
RT and reduction.";
RL J. Biol. Chem. 277:11513-11520(2002).
RN [4] {ECO:0007744|PDB:5J8D, ECO:0007744|PDB:5J8G}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH FMN AND THE NADH
RP ANALOG NAAD, AND COFACTOR.
RX PubMed=28578873; DOI=10.1016/j.str.2017.05.002;
RA Pitsawong W., Haynes C.A., Koder R.L., Rodgers D.W., Miller A.F.;
RT "Mechanism-Informed Refinement Reveals Altered Substrate-Binding Mode for
RT Catalytically Competent Nitroreductase.";
RL Structure 25:978-987(2017).
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.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:28578873};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11805110}.
CC -!- MISCELLANEOUS: The nitroreductase might be involved in the quinone
CC metabolism.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; M63808; AAA62801.1; -; Genomic_DNA.
DR PIR; A38686; A38686.
DR RefSeq; WP_024906901.1; NZ_QMCV01000003.1.
DR PDB; 1KQB; X-ray; 1.80 A; A/B/C/D=1-217.
DR PDB; 1KQC; X-ray; 1.80 A; A/B/C/D=1-217.
DR PDB; 1KQD; X-ray; 1.90 A; A/B/C/D=1-217.
DR PDB; 1NEC; X-ray; 1.95 A; A/B/C/D=2-217.
DR PDB; 5J8D; X-ray; 1.85 A; A/B/C/D=2-217.
DR PDB; 5J8G; X-ray; 1.90 A; A/B/C/D=2-217.
DR PDBsum; 1KQB; -.
DR PDBsum; 1KQC; -.
DR PDBsum; 1KQD; -.
DR PDBsum; 1NEC; -.
DR PDBsum; 5J8D; -.
DR PDBsum; 5J8G; -.
DR AlphaFoldDB; Q01234; -.
DR SMR; Q01234; -.
DR STRING; 1399774.JDWH01000007_gene1698; -.
DR DrugBank; DB03793; Benzoic acid.
DR DrugBank; DB03247; Flavin mononucleotide.
DR GeneID; 63141342; -.
DR eggNOG; COG0778; Bacteria.
DR BRENDA; 1.7.1.16; 155.
DR EvolutionaryTrace; Q01234; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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.
FT CHAIN 1..217
FT /note="Oxygen-insensitive NAD(P)H nitroreductase"
FT /id="PRO_0000072712"
FT BINDING 10..14
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:28578873,
FT ECO:0007744|PDB:5J8D"
FT BINDING 14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:28578873,
FT ECO:0007744|PDB:5J8D"
FT BINDING 41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:28578873,
FT ECO:0007744|PDB:5J8D"
FT BINDING 67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:28578873,
FT ECO:0007744|PDB:5J8D"
FT BINDING 71
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:28578873,
FT ECO:0007744|PDB:5J8D"
FT BINDING 71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:28578873,
FT ECO:0007744|PDB:5J8D"
FT BINDING 74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:28578873,
FT ECO:0007744|PDB:5J8D"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:28578873,
FT ECO:0007744|PDB:5J8D"
FT BINDING 165..166
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:28578873,
FT ECO:0007744|PDB:5J8D"
FT BINDING 205..207
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:28578873,
FT ECO:0007744|PDB:5J8D"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1KQB"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:1KQB"
FT STRAND 78..89
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 111..129
FT /evidence="ECO:0007829|PDB:1KQB"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 135..156
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:1KQB"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1KQB"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:1KQB"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1KQB"
SQ SEQUENCE 217 AA; 23950 MW; C42AA3DB184D5D9B CRC64;
MDIISVALKR HSTKAFDASK KLTAEEAEKI KTLLQYSPSS TNSQPWHFIV ASTEEGKARV
AKSAAGTYVF NERKMLDASH VVVFCAKTAM DDAWLERVVD QEEADGRFNT PEAKAANHKG
RTYFADMHRV DLKDDDQWMA KQVYLNVGNF LLGVGAMGLD AVPIEGFDAA ILDEEFGLKE
KGFTSLVVVP VGHHSVEDFN ATLPKSRLPL STIVTEC
