Protein

Oxygen-insensitive NAD(P)H nitroreductase

Gene

nfsB

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.1 Publication

Catalytic activityⁱ

5,6,7,8-tetrahydropteridine + NAD+ = 6,7-dihydropteridine + H+ + NADH

EC:1.5.1.34

Source: Rhea. « Hide
5,6,7,8-tetrahydropteridine

">zoom
+
NAD+

">zoom
=
6,7-dihydropteridine

">zoom
+
H+
+
NADH
5,6,7,8-tetrahydropteridine + NADP+ = 6,7-dihydropteridine + H+ + NADPH

EC:1.5.1.34

Source: Rhea. Show »

Cofactorⁱ

FMN

Activity regulationⁱ

Subject to competitive inhibition by dicoumarol, nicotinic acid and acetate with respect to NADH. Subject to uncompetitive inhibition by dicoumarol, nicotinic acid and acetate with respect to nitrofurazone and nitrofurantoin.1 Publication

Kineticsⁱ

K_M=350 µM for NADH1 Publication
K_M=1850 µM for nitrofurazone1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	41	NAD or NADP; via amide nitrogen		1
Binding siteⁱ	71	FMN3 Publications		1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	10 – 14	FMN3 Publications	5
Nucleotide bindingⁱ	153 – 158	NAD or NADPBy similarity	6
Nucleotide bindingⁱ	165 – 166	FMN3 Publications	2
Nucleotide bindingⁱ	205 – 207	FMN3 Publications	3

GO - Molecular functionⁱ

6,7-dihydropteridine reductase activity Source: EcoCyc
FMN binding Source: EcoCyc
identical protein binding Source: IntAct
NAD(P)H nitroreductase activity Source: EcoCyc
oxidoreductase activity Source: GO_Central

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

2,4,6-trinitrotoluene catabolic process Source: EcoCyc

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	Flavoprotein, FMN, NAD, NADP

Enzyme and pathway databases

BioCycⁱ

EcoCyc:DIHYDROPTERIREDUCT-MONOMER
MetaCyc:DIHYDROPTERIREDUCT-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Oxygen-insensitive NAD(P)H nitroreductase (EC:1.-.-.-) Alternative name(s): Dihydropteridine reductase (EC:1.5.1.34) FMN-dependent nitroreductase
Gene namesⁱ	Name:nfsB1 Publication Synonyms:dprA, nfnB1 Publication, nfsI, ntr Ordered Locus Names:b0578, JW0567
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol Source: EcoCyc
membrane Source: UniProtKB

Complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL1075080
DrugBankⁱ	DB04138, 5-[Bis(2-bromoethyl)amino]-N-(2,3-dioxopropyl)-2,4-dinitrobenzamide DB03228, 5-[Bis-2(Chloro-Ethyl)-Amino]-2,4-Dintro-Benzamide DB04392, Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone] DB03247, Flavin mononucleotide DB04253, Tretazicar

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000072711	1 – 217	Oxygen-insensitive NAD(P)H nitroreductaseAdd BLAST		217

Proteomic databases

jPOSTⁱ	P38489
PaxDbⁱ	P38489
PRIDEⁱ	P38489

2D gel databases

SWISS-2DPAGEⁱ

P38489

Interactionⁱ

Subunit structureⁱ

Homodimer.

4 Publications

Binary interactionsⁱ

P38489

With	#Exp.	IntAct
itself	2	EBI-909296,EBI-909296

GO - Molecular functionⁱ

identical protein binding Source: IntAct

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	4262913, 20 interactors 850145, 1 interactor
DIPⁱ	DIP-10330N
IntActⁱ	P38489, 12 interactors
STRINGⁱ	511145.b0578

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

3D structure databases

SMRⁱ	P38489
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P38489

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the nitroreductase family.Curated

Phylogenomic databases

eggNOGⁱ	COG0778, Bacteria
HOGENOMⁱ	CLU_070764_4_1_6
InParanoidⁱ	P38489
PhylomeDBⁱ	P38489

Family and domain databases

CDDⁱ	cd02149, NfsB_like_nitroreductase, 1 hit
Gene3Dⁱ	3.40.109.10, 1 hit
InterProⁱ	View protein in InterPro IPR033878, NfsB-like IPR029479, Nitroreductase IPR000415, Nitroreductase-like
Pfamⁱ	View protein in Pfam PF00881, Nitroreductase, 1 hit
SUPFAMⁱ	SSF55469, SSF55469, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P38489-1 [UniParc]FASTAAdd to basket

« Hide

10         20         30         40         50MDIISVALKR HSTKAFDASK KLTPEQAEQI KTLLQYSPSS TNSQPWHFIV         60         70         80         90        100ASTEEGKARV AKSAAGNYVF NERKMLDASH VVVFCAKTAM DDVWLKLVVD        110        120        130        140        150QEDADGRFAT PEAKAANDKG RKFFADMHRK DLHDDAEWMA KQVYLNVGNF        160        170        180        190        200LLGVAALGLD AVPIEGFDAA ILDAEFGLKE KGYTSLVVVP VGHHSVEDFN        210 ATLPKSRLPQ NITLTEV

Length:217

Mass (Da):23,905

Last modified:October 1, 1994 - v1

Checksum:ⁱA516CEFC3D46AEAC

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	5	S → C AA sequence (PubMed:3060113).Curated	1
Sequence conflictⁱ	10 – 12	RHS → CIV AA sequence (PubMed:3060113).Curated	3
Sequence conflictⁱ	19	S → M AA sequence (PubMed:3060113).Curated	1
Sequence conflictⁱ	21	Missing AA sequence (PubMed:1472094).Curated	1
Sequence conflictⁱ	28	E → D AA sequence (PubMed:1472094).Curated	1
Sequence conflictⁱ	180	E → I AA sequence (PubMed:1472094).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ	D25414 Genomic DNA Translation: BAA05004.1 U07860 Genomic DNA Translation: AAC43263.1 U82598 Genomic DNA Translation: AAB40776.1 U00096 Genomic DNA Translation: AAC73679.1 AP009048 Genomic DNA Translation: BAA35218.1
PIRⁱ	I67685 S01818
RefSeqⁱ	NP_415110.1, NC_000913.3 WP_000351487.1, NZ_SSZK01000024.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73679; AAC73679; b0578 BAA35218; BAA35218; BAA35218
GeneIDⁱ	945778
KEGGⁱ	ecj:JW0567 eco:b0578
PATRICⁱ	fig\|1411691.4.peg.1696

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins	Species	Length	Source
P38489	Dihydropteridine reductase, NAD(P)H-dependent, oxygen-insensitive	uncultured bacterium Contigcl_1559	217	UniRef100_P38489
	Oxygen-insensitive NAD(P)H nitroreductase	Escherichia coli HVH 101 (4-6859844)	217
	Dihydropteridine reductase	ECOLX	217
	Oxygen-insensitive NAD(P)H nitroreductase	Salmonella sp. HNK130	217
	Oxygen-insensitive NAD(P)H nitroreductase (FMN-dependentnitroreductase) (Dihydropteridine reductase)	Escherichia coli H386	217
	+11

Full view

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ	D25414 Genomic DNA Translation: BAA05004.1 U07860 Genomic DNA Translation: AAC43263.1 U82598 Genomic DNA Translation: AAB40776.1 U00096 Genomic DNA Translation: AAC73679.1 AP009048 Genomic DNA Translation: BAA35218.1
PIRⁱ	I67685 S01818
RefSeqⁱ	NP_415110.1, NC_000913.3 WP_000351487.1, NZ_SSZK01000024.1

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1DS7	X-ray	2.06	A/B	1-217	[»]
	1ICR	X-ray	1.70	A/B	1-217	[»]
	1ICU	X-ray	1.80	A/B/C/D	1-217	[»]
	1ICV	X-ray	2.40	A/B/C/D	1-217	[»]
	1IDT	X-ray	2.00	A/B	1-217	[»]
	1OO5	X-ray	2.50	A/B	1-217	[»]
	1OO6	X-ray	2.00	A/B	1-217	[»]
	1OON	X-ray	2.49	A/B	1-217	[»]
	1OOQ	X-ray	2.00	A/B	1-217	[»]
	1YKI	X-ray	1.70	A/B/C/D	1-217	[»]
	1YLR	X-ray	1.70	A/B	1-217	[»]
	1YLU	X-ray	2.00	A/B	1-217	[»]
	3X21	X-ray	3.00	A/B/C/D/E/F/G/H/I/J	1-217	[»]
	3X22	X-ray	2.00	A/B	1-217	[»]
SMRⁱ	P38489
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	4262913, 20 interactors 850145, 1 interactor
DIPⁱ	DIP-10330N
IntActⁱ	P38489, 12 interactors
STRINGⁱ	511145.b0578

Chemistry databases

ChEMBLⁱ	CHEMBL1075080
DrugBankⁱ	DB04138, 5-[Bis(2-bromoethyl)amino]-N-(2,3-dioxopropyl)-2,4-dinitrobenzamide DB03228, 5-[Bis-2(Chloro-Ethyl)-Amino]-2,4-Dintro-Benzamide DB04392, Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone] DB03247, Flavin mononucleotide DB04253, Tretazicar

2D gel databases

SWISS-2DPAGEⁱ

P38489

Proteomic databases

jPOSTⁱ	P38489
PaxDbⁱ	P38489
PRIDEⁱ	P38489

Genome annotation databases

EnsemblBacteriaⁱ	AAC73679; AAC73679; b0578 BAA35218; BAA35218; BAA35218
GeneIDⁱ	945778
KEGGⁱ	ecj:JW0567 eco:b0578
PATRICⁱ	fig\|1411691.4.peg.1696

Organism-specific databases

EchoBASEⁱ

EB4146

Phylogenomic databases

eggNOGⁱ	COG0778, Bacteria
HOGENOMⁱ	CLU_070764_4_1_6
InParanoidⁱ	P38489
PhylomeDBⁱ	P38489

Enzyme and pathway databases

BioCycⁱ

EcoCyc:DIHYDROPTERIREDUCT-MONOMER
MetaCyc:DIHYDROPTERIREDUCT-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P38489
PROⁱ	PR:P38489

Family and domain databases

CDDⁱ	cd02149, NfsB_like_nitroreductase, 1 hit
Gene3Dⁱ	3.40.109.10, 1 hit
InterProⁱ	View protein in InterPro IPR033878, NfsB-like IPR029479, Nitroreductase IPR000415, Nitroreductase-like
Pfamⁱ	View protein in Pfam PF00881, Nitroreductase, 1 hit
SUPFAMⁱ	SSF55469, SSF55469, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	NFSB_ECOLI
Accessionⁱ	Primary (citable) accession number: P38489 Secondary accession number(s): P19575
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
	Last sequence update:	October 1, 1994
	Last modified:	December 2, 2020
	This is version 169 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

nfsB

Oxygen-insensitive NAD(P)H nitroreductase

nfsB

Functioni

Catalytic activityi

Cofactori

Activity regulationi

Kineticsi

Sites

Regions

GO - Molecular functioni

GO - Biological processi

Keywordsi

Enzyme and pathway databases

Names & Taxonomyi

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Chemistry databases

PTM / Processingi

Molecule processing

Proteomic databases

2D gel databases

Interactioni

Subunit structurei

Binary interactionsi

P38489

GO - Molecular functioni

Protein-protein interaction databases

Structurei

Secondary structure

3D structure databases

Miscellaneous databases

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequencei

Experimental Info

Sequence databases

Genome annotation databases

Similar proteinsi

Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

2D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

Entry informationi

Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

Cofactorⁱ

Activity regulationⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Keywordsⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Subunit structureⁱ

Binary interactionsⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Similar proteinsⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ