[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-26. STRAIN=K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222; PubMed=8449868 [NCBI, ExPASy, EBI, Israel, Japan] Bianchi V., Reichard P., Eliasson R., Pontis E., Krook M., Joernvall H., Haggaard-Ljungquist E.; "Escherichia coli ferredoxin NADP+ reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), and overexpression of the protein."; J. Bacteriol. 175:1590-1595(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/21.15.3391; PubMed=8346018 [NCBI, ExPASy, EBI, Israel, Japan] Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.; "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."; Nucleic Acids Res. 21:3391-3398(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135. STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; PubMed=1400248 [NCBI, ExPASy, EBI, Israel, Japan] Truniger V., Boos W., Sweet G.; "Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri."; J. Bacteriol. 174:6981-6991(1992).
[6]	PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129. STRAIN=K12; PubMed=2834327 [NCBI, ExPASy, EBI, Israel, Japan] Morimyo M.; "Isolation and characterization of methyl viologen-sensitive mutants of Escherichia coli K-12."; J. Bacteriol. 170:2136-2142(1988).
[7]	PROTEIN SEQUENCE OF 2-14. PubMed=7961651 [NCBI, ExPASy, EBI, Israel, Japan] Jenkins C.M., Waterman M.R.; "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities."; J. Biol. Chem. 269:27401-27408(1994).
[8]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). DOI=10.1006/jmbi.1997.0957; PubMed=9149148 [NCBI, ExPASy, EBI, Israel, Japan] Ingelman M., Blanchi V., Eklund H.; "The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7-A resolution."; J. Mol. Biol. 268:147-157(1997).

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: Monomer.
SIMILARITY: Belongs to the ferredoxin--NADP reductase family.
SIMILARITY: 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:
- Sequence=Z11767; Type=Frameshift; Positions=94, 127;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L04757; AAA23805.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L19201; AAB03056.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76906.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77386.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z11767; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M19644; AAA24189.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S40867; S40867.

RefSeq

AP_003885.1; -.
NP_418359.1; -.

3D structure databases

PDB

1FDR; X-ray; 1.70 A; A=1-248.

[ExPASy / RCSB / EBI]

PDBsum

1FDR; -.

ModBase

P28861.

Enzyme and pathway databases

BioCyc

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

Organism-specific databases

EchoBASE

EB1480; -.

EcoGene

EG11518; fpr.

Ontologies

GO:0004324;	Molecular function: ferredoxin-NADP+ reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

Pfam

PF00970; FAD_binding_6; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PROSITE

PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

948414; -.

GenomeReviews

U00096_GR; b3924.
AP009048_GR; JW3895.

KEGG

ecj:JW3895; -.
eco:b3924; -.

Phylogenomic databases

HOGENOM

P28861; -.

Other

LinkHub

P28861; -.

Genome annotation databases

CMR

P28861; b3924.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 248`	`247`	`Ferredoxin--NADP reductase.`	`PRO_0000167643`
`DOMAIN`	`2 101`	`100`	`FAD-binding FR-type.`
`NP_BIND`	`50 76`	`27`	`FAD.`
`NP_BIND`	`110 126`	`17`	`NADP (By similarity).`
`STRAND`	`4 14`	`11`
`STRAND`	`16 25`	`10`
`STRAND`	`36 41`	`6`
`STRAND`	`48 53`	`6`
`STRAND`	`61 68`	`8`
`HELIX`	`76 80`	`5`
`STRAND`	`87 93`	`7`
`HELIX`	`100 102`	`3`
`STRAND`	`107 114`	`8`
`HELIX`	`115 118`	`4`
`HELIX`	`119 127`	`9`
`STRAND`	`135 145`	`11`
`HELIX`	`146 148`	`3`
`HELIX`	`152 161`	`10`
`TURN`	`162 164`	`3`
`STRAND`	`165 175`	`11`
`STRAND`	`180 183`	`4`
`HELIX`	`185 190`	`6`
`HELIX`	`193 198`	`6`
`TURN`	`204 206`	`3`
`STRAND`	`207 213`	`7`
`HELIX`	`215 229`	`15`
`STRAND`	`241 246`	`6`

Sequence information

Length: 248 AA [This is the length of the unprocessed precursor]

Molecular weight: 27751 Da [This is the MW of the unprocessed precursor]

CRC64: CBF46435A95709E4 [This is a checksum on the sequence]

        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

P28861 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools