[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=301 / Serotype 2a; DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan] Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."; Nucleic Acids Res. 30:4432-4441(2002).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 700930 / 2457T / Serotype 2a; DOI=10.1128/IAI.71.5.2775-2786.2003; PubMed=12704152 [NCBI, ExPASy, EBI, Israel, Japan] Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."; Infect. Immun. 71:2775-2786(2003).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135. STRAIN=M4243; 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).

Comments

FUNCTION: Together with flavodoxin is 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 (By similarity).
CATALYTIC ACTIVITY: 2 reduced ferredoxin + NADP⁺ + H⁺ = 2 oxidized ferredoxin + NADPH.
COFACTOR: FAD.
SIMILARITY: Belongs to the ferredoxin--NADP reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SEQUENCE CAUTION:
- Sequence=CAA77813.1; Type=Frameshift; Positions=94, 126;

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

AE005674; AAN45435.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP18765.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z11766; CAA77813.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S23906; S23906.

RefSeq

NP_709728.1; -.
NP_838954.1; -.

3D structure databases

HSSP

P28861; 1FDR. [HSSP ENTRY / PDB]

SMR

P28901; 2-248.

ModBase

P28901.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN45435.1-MON; -.

Ontologies

GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
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).

ProtoNet

P28901.

Genome annotation databases

GeneID

1023471; -.
1079956; -.

GenomeReviews

AE014073_GR; S3745.
AE005674_GR; SF4002.

KEGG

sfl:SF4002; -.
sfx:S3745; -.

Phylogenomic databases

HOGENOM

P28901; -.

Genome annotation databases

CMR

P28901; SF4002.

Other

UniRef

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

Keywords

Complete proteome; FAD; Flavoprotein; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 248`	`248`	`Ferredoxin--NADP reductase.`	`PRO_0000167644`
`DOMAIN`	`2 101`	`100`	`FAD-binding FR-type.`
`NP_BIND`	`50 76`	`27`	`FAD (By similarity).`
`NP_BIND`	`110 126`	`17`	`NADP (By similarity).`

Sequence information

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

Molecular weight: 27699 Da [This is the MW of the unprocessed precursor]

CRC64: 1D71D26F195EA512 [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 DEVPDCETLW MLATGTAIGP 

       130        140        150        160        170        180 
YLSILQLGKD LDRFKNLVLV HAARYAADLS YLPLMQELEK RYEGKLRIQT VVSRETAAGS 

       190        200        210        220        230        240 
LTGRIPALIE SGELESAIGL PMNKETSHVM LCGNPQMVRD TQQLLKETRQ MTKHLRRRPG 


HMTAEHYW

P28901 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