nfsA

Functionⁱ

Catalyzes the reduction of nitroaromatic compounds using NADPH. Has a broad electron acceptor specificity. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major oxygen-insensitive nitroreductase in E.coli.1 Publication

Cofactorⁱ

FMN2 PublicationsNote: Binds 1 FMN per monomer.1 Publication

Kineticsⁱ

K_M=
11 µM for NADPH
1 Publication
Manual assertion based on experiment inⁱ
- Ref.2
  "Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase."
  Zenno S., Koike H., Kumar A.N., Jayaraman R., Tanokura M., Saigo K.
  J. Bacteriol. 178:4508-4514(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
5.5 µM for nitrofurazone
1 Publication
Manual assertion based on experiment inⁱ
- Ref.2
  "Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase."
  Zenno S., Koike H., Kumar A.N., Jayaraman R., Tanokura M., Saigo K.
  J. Bacteriol. 178:4508-4514(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	39	FMN; via amide nitrogenCombined sources1 Publication		1
Binding siteⁱ	67	FMNCombined sources1 Publication		1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	11 – 15	FMNCombined sources1 Publication	5
Nucleotide bindingⁱ	128 – 131	FMNCombined sources1 Publication	4
Nucleotide bindingⁱ	167 – 169	FMNCombined sources1 Publication	3

GO - Molecular functionⁱ

chromate reductase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 15250887
FMN binding
Source: EcoCyc
Inferred from direct assayⁱ
- 8755878
oxidoreductase activity, acting on NAD(P)H, nitrogenous group as acceptor
Source: EcoCyc
Inferred from direct assayⁱ
- 8755878

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	Flavoprotein, FMN, NADP

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11261-MONOMER MetaCyc:EG11261-MONOMER

BioCycⁱ

EcoCyc:EG11261-MONOMER
MetaCyc:EG11261-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Oxygen-insensitive NADPH nitroreductaseCurated (EC:1.-.-.-1 Publication) Alternative name(s): Modulator of drug activity A
Gene namesⁱ	Name:nfsA Synonyms:mda18, mdaA1 Publication, ybjB Ordered Locus Names:b0851, JW0835
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11261 nfsA

EcoGeneⁱ

EG11261 nfsA

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 18304323

View the complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	203	R → A: Strong decrease in activity. 1 Publication		1
Mutagenesisⁱ	208	R → A: No change in activity. 1 Publication		1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB00698 Nitrofurantoin DB03247 Riboflavin Monophosphate

DrugBankⁱ

DB00698 Nitrofurantoin
DB03247 Riboflavin Monophosphate

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000205510	1 – 240	Oxygen-insensitive NADPH nitroreductaseAdd BLAST		240

Proteomic databases

EPDⁱ	P17117
PaxDbⁱ	P17117
PRIDEⁱ	P17117

Interactionⁱ

Subunit structureⁱ

Homodimer.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
holA	P28630	3	EBI-1120624,EBI-549153

With

Entry

#Exp.

IntAct

Notes

holA

P28630

3

EBI-1120624,EBI-549153

Protein-protein interaction databases

BioGridⁱ	4259991, 28 interactors
Database of interacting proteins More...DIPⁱ	DIP-10334N
IntActⁱ	P17117, 5 interactors
STRINGⁱ	316385.ECDH10B_0921

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 9	Combined sources	7
Helixⁱ	24 – 35	Combined sources	12
Helixⁱ	40 – 42	Combined sources	3
Beta strandⁱ	46 – 50	Combined sources	5
Helixⁱ	54 – 63	Combined sources	10
Helixⁱ	69 – 72	Combined sources	4
Beta strandⁱ	73 – 82	Combined sources	10
Helixⁱ	84 – 89	Combined sources	6
Helixⁱ	98 – 121	Combined sources	24
Beta strandⁱ	125 – 129	Combined sources	5
Helixⁱ	130 – 135	Combined sources	6
Helixⁱ	136 – 142	Combined sources	7
Beta strandⁱ	149 – 158	Combined sources	10
Helixⁱ	172 – 175	Combined sources	4
Beta strandⁱ	176 – 180	Combined sources	5
Helixⁱ	186 – 201	Combined sources	16
Helixⁱ	212 – 220	Combined sources	9
Helixⁱ	228 – 234	Combined sources	7

Show more details

3D structure databases

ProteinModelPortalⁱ	P17117
SMRⁱ	P17117
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P17117

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the flavin oxidoreductase frp family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4108DBC Bacteria COG0778 LUCA
HOGENOMⁱ	HOG000272869
InParanoidⁱ	P17117
KEGG Orthology (KO) More...KOⁱ	K10678
PhylomeDBⁱ	P17117

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd02146 NfsA_FRP, 1 hit
Gene3Dⁱ	3.40.109.10, 1 hit
InterProⁱ	View protein in InterPro IPR016446 Flavin_OxRdtase_Frp IPR029479 Nitroreductase IPR000415 Nitroreductase-like
PANTHERⁱ	PTHR43425 PTHR43425, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00881 Nitroreductase, 1 hit
PIRSFⁱ	PIRSF005426 Frp, 1 hit
SUPFAMⁱ	SSF55469 SSF55469, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P17117-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTPTIELICG HRSIRHFTDE PISEAQREAI INSARATSSS SFLQCSSIIR 
        60         70         80         90        100
ITDKALREEL VTLTGGQKHV AQAAEFWVFC ADFNRHLQIC PDAQLGLAEQ 
       110        120        130        140        150
LLLGVVDTAM MAQNALIAAE SLGLGGVYIG GLRNNIEAVT KLLKLPQHVL 
       160        170        180        190        200
PLFGLCLGWP ADNPDLKPRL PASILVHENS YQPLDKGALA QYDEQLAEYY 
       210        220        230        240
LTRGSNNRRD TWSDHIRRTI IKESRPFILD YLHKQGWATR

Length:240

Mass (Da):26,801

Last modified:February 1, 1995 - v2

Checksum:ⁱ3B389FCDB86DED1D

GO

Sequence cautionⁱ

The sequence CAA33867 differs from that shown. Reason: Frameshift at positions 155, 161 and 187.Curated

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U18655 Genomic DNA Translation: AAC43450.1 D38308 Genomic DNA Translation: BAA07425.1 U00096 Genomic DNA Translation: AAC73938.1 AP009048 Genomic DNA Translation: BAA35562.1 X15859 Genomic DNA Translation: CAA33867.1 Frameshift.
PIRⁱ	I80318
NCBI Reference Sequences More...RefSeqⁱ	NP_415372.1, NC_000913.3 WP_000189159.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73938; AAC73938; b0851 BAA35562; BAA35562; BAA35562
GeneIDⁱ	945483
KEGGⁱ	ecj:JW0835 eco:b0851
PATRICⁱ	fig\|1411691.4.peg.1427

Protein	Similar proteins		Species	Score	Length	Source
P17117	NADPH-dependent oxidoreductase		Shigella sp.		240	UniRef100_P17117
Oxygen-insensitive NADPH nitroreductase		Klebsiella pneumoniae IS22		240
Oxygen-insensitive NADPH nitroreductase		KLEPN		240
NADPH-dependent oxidoreductase		Escherichia coli M8		240
Modulator of drug activity A		ECOLX		240
+37

Protein	Similar proteins		Species	Score	Length	Source
P17117	NADPH-dependent oxidoreductase		Shigella sp.		240	UniRef90_P17117
Oxygen-insensitive NADPH nitroreductase		Klebsiella pneumoniae IS22		240
Oxygen-insensitive NADPH nitroreductase		KLEPN		240
NADPH-dependent oxidoreductase		Escherichia coli M8		240
Modulator of drug activity A		ECOLX		240
+817

Protein	Similar proteins		Species	Score	Length	Source
P17117	NADPH-dependent oxidoreductase		Shigella sp.		240	UniRef50_P17117
Oxygen-insensitive NADPH nitroreductase		Klebsiella pneumoniae IS22		240
Oxygen-insensitive NADPH nitroreductase		KLEPN		240
NADPH-dependent oxidoreductase		Escherichia coli M8		240
Modulator of drug activity A		ECOLX		240
+1121

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U18655 Genomic DNA Translation: AAC43450.1 D38308 Genomic DNA Translation: BAA07425.1 U00096 Genomic DNA Translation: AAC73938.1 AP009048 Genomic DNA Translation: BAA35562.1 X15859 Genomic DNA Translation: CAA33867.1 Frameshift.
PIRⁱ	I80318
RefSeqⁱ	NP_415372.1, NC_000913.3 WP_000189159.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1F5V	X-ray	1.70	A/B	1-240	[»]
ProteinModelPortalⁱ	P17117
SMRⁱ	P17117
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4259991, 28 interactors
DIPⁱ	DIP-10334N
IntActⁱ	P17117, 5 interactors
STRINGⁱ	316385.ECDH10B_0921

Chemistry databases

DrugBankⁱ	DB00698 Nitrofurantoin DB03247 Riboflavin Monophosphate

DrugBankⁱ

DB00698 Nitrofurantoin
DB03247 Riboflavin Monophosphate

Proteomic databases

EPDⁱ	P17117
PaxDbⁱ	P17117
PRIDEⁱ	P17117

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73938; AAC73938; b0851 BAA35562; BAA35562; BAA35562
GeneIDⁱ	945483
KEGGⁱ	ecj:JW0835 eco:b0851
PATRICⁱ	fig\|1411691.4.peg.1427

Organism-specific databases

EchoBASEⁱ	EB1241
EcoGeneⁱ	EG11261 nfsA

Phylogenomic databases

eggNOGⁱ	ENOG4108DBC Bacteria COG0778 LUCA
HOGENOMⁱ	HOG000272869
InParanoidⁱ	P17117
KOⁱ	K10678
PhylomeDBⁱ	P17117

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11261-MONOMER MetaCyc:EG11261-MONOMER

BioCycⁱ

EcoCyc:EG11261-MONOMER
MetaCyc:EG11261-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P17117
Protein Ontology More...PROⁱ	PR:P17117

Family and domain databases

CDDⁱ	cd02146 NfsA_FRP, 1 hit
Gene3Dⁱ	3.40.109.10, 1 hit
InterProⁱ	View protein in InterPro IPR016446 Flavin_OxRdtase_Frp IPR029479 Nitroreductase IPR000415 Nitroreductase-like
PANTHERⁱ	PTHR43425 PTHR43425, 1 hit
Pfamⁱ	View protein in Pfam PF00881 Nitroreductase, 1 hit
PIRSFⁱ	PIRSF005426 Frp, 1 hit
SUPFAMⁱ	SSF55469 SSF55469, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	NFSA_ECOLI
Accessionⁱ	P17117Primary (citable) accession number: P17117
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
	Last sequence update:	February 1, 1995
	Last modified:	November 7, 2018
	This is version 144 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P17117 (NFSA_ECOLI)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Oxygen-insensitive NADPH nitroreductase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ