Reviewed, UniProtKB/Swiss-Prot P28861 (FENR_ECOLI)

Names and origin

Protein names

Recommended name:
    Ferredoxin--NADP reductase
      Short name=FNR
    EC=1.18.1.2
Alternative name(s):
    Flavodoxin reductase
      Short name=FLXR
      Short name=FLDR
    Methyl viologen resistance protein A
    DA1

Gene names

Name:	fpr
Synonyms:	mvrA
Ordered Locus Names:	b3924, JW3895

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transports electrons between flavodoxin or ferredoxin and NADPH. Involved in the reductive activation of cobalamin-independent methionine synthase, pyruvate formate lyase and anaerobic ribonucleotide reductase. Also protects against superoxide radicals due to methyl viologen in the presence of oxygen.
Catalytic activity	2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.
Cofactor	FAD.
Subunit structure	Monomer.
Sequence similarities	Belongs to the ferredoxin--NADP reductase type 1 family. Contains 1 FAD-binding FR-type domain.
Caution	Ref.6 authors incorrectly assigned the protein to be part of FPR, the C-terminal of glpX.
Sequence caution	The sequence Z11767 differs from that shown. Reason: Frameshift at positions 94 and 127.

Ontologies

Keywords
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro ferredoxin-NADP+ reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1 Ref.7

Chain

2 – 248

247

Ferredoxin--NADP reductase

PRO_0000167643

Regions

Domain

2 – 101

100

FAD-binding FR-type

Nucleotide binding

50 – 53

4

FAD

Nucleotide binding

74 – 76

3

FAD

Nucleotide binding

143 – 144

2

NADP By similarity

Nucleotide binding

173 – 174

2

NADP By similarity

Nucleotide binding

213 – 214

2

NADP By similarity

Nucleotide binding

247 – 248

2

FAD

Sites

Binding site

53

1

NADP By similarity

Binding site

66

1

FAD; via carbonyl oxygen

Binding site

116

1

FAD

Binding site

116

1

NADP; via amide nitrogen By similarity

Binding site

245

1

NADP By similarity

Secondary structure

1

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248

Helix Strand Turn

Details...

Beta strand

4 – 14

11

Beta strand

16 – 25

10

Beta strand

36 – 41

6

Beta strand

48 – 53

6

Beta strand

61 – 68

8

Helix

76 – 80

5

Beta strand

87 – 93

7

Helix

100 – 102

3

Beta strand

107 – 114

8

Helix

115 – 118

4

Helix

119 – 127

9

Beta strand

135 – 145

11

Helix

146 – 148

3

Helix

152 – 161

10

Turn

162 – 164

3

Beta strand

165 – 175

11

Beta strand

180 – 183

4

Helix

185 – 190

6

Helix

193 – 198

6

Turn

204 – 206

3

Beta strand

207 – 213

7

Helix

215 – 229

15

Beta strand

241 – 246

6

Sequences

	Sequence		Length	Mass (Da)
	P28861-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: CBF46435A95709E4	FASTA	248	27,751
	10 20 30 40 50 60 MADWVTGKVT KVQNWTDALF SLTVHAPVLP FTAGQFTKLG LEIDGERVQR AYSYVNSPDN 70 80 90 100 110 120 PDLEFYLVTV PDGKLSPRLA ALKPGDEVQV VSEAAGFFVL DEVPHCETLW MLATGTAIGP 130 140 150 160 170 180 YLSILQLGKD LDRFKNLVLV HAARYAADLS YLPLMQELEK RYEGKLRIQT VVSRETAAGS 190 200 210 220 230 240 LTGRIPALIE SGELESTIGL PMNKETSHVM LCGNPQMVRD TQQLLKETRQ MTKHLRRRPG HMTAEHYW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Escherichia coli ferredoxin NADP+ reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), and overexpression of the protein." Bianchi V., Reichard P., Eliasson R., Pontis E., Krook M., Joernvall H., Haggaard-Ljungquist E. J. Bacteriol. 175:1590-1595(1993) [PubMed: 8449868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26. Strain: K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222.
[2]	"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Plunkett G. III, Burland V., Daniels D.L., Blattner F.R. Nucleic Acids Res. 21:3391-3398(1993) [PubMed: 8346018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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.
[4]	"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.
[5]	"Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri." Truniger V., Boos W., Sweet G. J. Bacteriol. 174:6981-6991(1992) [PubMed: 1400248] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[6]	"Isolation and characterization of methyl viologen-sensitive mutants of Escherichia coli K-12." Morimyo M. J. Bacteriol. 170:2136-2142(1988) [PubMed: 2834327] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129. Strain: K12.
[7]	"Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities." Jenkins C.M., Waterman M.R. J. Biol. Chem. 269:27401-27408(1994) [PubMed: 7961651] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14.
[8]	"The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7-A resolution." Ingelman M., Blanchi V., Eklund H. J. Mol. Biol. 268:147-157(1997) [PubMed: 9149148] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FAD.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L04757 Genomic DNA. Translation: AAA23805.1.
L19201 Genomic DNA. Translation: AAB03056.1.
U00096 Genomic DNA. Translation: AAC76906.1.
AP009048 Genomic DNA. Translation: BAE77386.1.
Z11767 Genomic DNA. No translation available.
M19644 Genomic DNA. Translation: AAA24189.1. Sequence problems.

PIR

S40867.

RefSeq

AP_003885.1.
NP_418359.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FDR	X-ray	1.70	A	1-248	[»]

ModBase

Search...

Genome annotation databases

GeneID

948414.

GenomeReviews

Gene locus JW3895 in contig AP009048_GR.
Gene locus b3924 in contig U00096_GR.

KEGG

ecj:JW3895.
eco:b3924.

Organism-specific databases

EchoBASE

EB1480.

EcoGene

EG11518. fpr.

CMR

Search...

Phylogenomic databases

HOGENOM

P28861.

OMA

P28861. IMLCGNP.

Enzyme and pathway databases

BioCyc

EcoCyc:FLAVONADPREDUCT-MON.
MetaCyc:FLAVONADPREDUCT-MON.

Family and domain databases

InterPro

IPR017927. Fd_Rdtase_FAD-bd.
IPR008333. OxRdtase_FAD-bd.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]

Pfam

PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]

PROSITE

PS51384. FAD_FR. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FENR_ECOLI

Accession

Primary (citable) accession number: P28861
Secondary accession number(s): P11007, Q2M8M0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 86 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)