P17117 (NFSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Oxygen-insensitive NADPH nitroreductase
EC=1.-.-.-

Alternative name(s):
Modulator of drug activity A

Gene names

Name:	nfsA
Synonyms:	mda18, mdaA, ybjB
Ordered Locus Names:	b0851, JW0835

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	240 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Reduction of nitroaromatic compounds using NADH. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major component of the oxygen-insensitive nitroreductase activity in E.coli.
Cofactor	FMN.
Sequence similarities	Belongs to the flavin oxidoreductase frp family.
Sequence caution	The sequence CAA33867.1 differs from that shown. Reason: Frameshift at positions 155, 161 and 187.

Ontologies

Keywords
Ligand	FMN Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dnaK	P0A6Y8	1	EBI-1120624,EBI-542092

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 240

240

Oxygen-insensitive NADPH nitroreductase

PRO_0000205510

Secondary structure

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240

Helix Strand Turn

Details...

Helix

3 – 9

7

Helix

24 – 35

12

Helix

40 – 42

3

Beta strand

46 – 50

5

Helix

54 – 63

10

Helix

69 – 72

4

Beta strand

73 – 82

10

Helix

84 – 89

6

Helix

98 – 121

24

Beta strand

125 – 129

5

Helix

130 – 135

6

Helix

136 – 142

7

Beta strand

149 – 158

10

Helix

172 – 175

4

Beta strand

176 – 180

5

Helix

186 – 201

16

Helix

212 – 220

9

Helix

228 – 234

7

Sequences

	Sequence		Length	Mass (Da)
	P17117 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 3B389FCDB86DED1D	FASTA	240	26,801
	10 20 30 40 50 60 MTPTIELICG HRSIRHFTDE PISEAQREAI INSARATSSS SFLQCSSIIR ITDKALREEL 70 80 90 100 110 120 VTLTGGQKHV AQAAEFWVFC ADFNRHLQIC PDAQLGLAEQ LLLGVVDTAM MAQNALIAAE 130 140 150 160 170 180 SLGLGGVYIG GLRNNIEAVT KLLKLPQHVL PLFGLCLGWP ADNPDLKPRL PASILVHENS 190 200 210 220 230 240 YQPLDKGALA QYDEQLAEYY LTRGSNNRRD TWSDHIRRTI IKESRPFILD YLHKQGWATR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A general genetic approach in Escherichia coli for determining the mechanism(s) of action of tumoricidal agents: application to DMP 840, a tumoricidal agent." Chatterjee P.K., Sternberg N.L. Proc. Natl. Acad. Sci. U.S.A. 92:8950-8954(1995) [PubMed: 7568050] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 8755878] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / AB1157.
[3]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12." Kang W.-K., Icho T., Isono S., Kitakawa M., Isono K. Mol. Gen. Genet. 217:281-288(1989) [PubMed: 2570347] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-240. Strain: K12.
[7]	"Conversion of NfsA, the major Escherichia coli nitroreductase, to a flavin reductase with an activity similar to that of Frp, a flavin reductase in Vibrio harveyi, by a single amino acid substitution." Zenno S., Kobori T., Tanokura M., Saigo K. J. Bacteriol. 180:422-425(1998) [PubMed: 9440535] [Abstract] Cited for: MUTAGENESIS.
[8]	"Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution." Kobori T., Sasaki H., Lee W.C., Zenno S., Saigo K., Murphy M.E., Tanokura M. J. Biol. Chem. 276:2816-2823(2001) [PubMed: 11034992] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

I80318.

RefSeq

NP_415372.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F5V	X-ray	1.70	A/B	1-240	[»]

ProteinModelPortal

P17117.

SMR

P17117. Positions 1-240.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10334N.

IntAct

P17117. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001563; EBESCP00000001563; EBESCG00000001297.
EBESCT00000017008; EBESCP00000016299; EBESCG00000016067.

GeneID

945483.

GenomeReviews

Gene locus JW0835 in contig AP009048_GR.
Gene locus b0851 in contig U00096_GR.

KEGG

ecj:JW0835.
eco:b0851.

PATRIC

32116907. VBIEscCol129921_0879.

Organism-specific databases

EchoBASE

EB1241.

EcoGene

EG11261. nfsA.

Phylogenomic databases

eggNOG

COG0778.

GeneTree

EBGT00050000011514.

HOGENOM

HBG532063.

OMA

HENGYDE.

PhylomeDB

P17117.

ProtClustDB

PRK10765.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11261-MONOMER.
MetaCyc:EG11261-MONOMER.

Gene expression databases

Genevestigator

P17117.

Family and domain databases

InterPro

IPR016446. Nitro/flavin_Rdtase.
IPR000415. Nitroreductase-like.
[Graphical view]

Gene3D

G3DSA:3.40.109.10. G3DSA:3.40.109.10. 1 hit.

KO

K10678.

Pfam

PF00881. Nitroreductase. 1 hit.
[Graphical view]

PIRSF

PIRSF005426. Frp. 1 hit.

SUPFAM

SSF55469. Nitroreductase. 1 hit.

ProtoNet

Search...

Other

DrugBank

DB00698. Nitrofurantoin.

Entry information

Entry name

NFSA_ECOLI

Accession

Primary (citable) accession number: P17117

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program