Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P41346 (FENR_VICFA)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Ferredoxin--NADP reductase, chloroplastic
      Short name=FNR
    EC=1.18.1.2
Gene names
Name: PETH
OrganismVicia faba (Broad bean)
Taxonomic identifier3906 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Vicia

Hide | Top

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

Hide | Top

General annotation (Comments)

Function

May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.

Catalytic activity

2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.

Cofactor

FAD.

Pathway

Energy metabolism; photosynthesis.

Subcellular location

Plastid › chloroplast stroma. Plastid › chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side Probable. Note: In the vicinity of the photosystem I in the non-stacked and fringe portion of the membrane.

Sequence similarities

Belongs to the ferredoxin--NADP reductase type 1 family.

Contains 1 FAD-binding FR-type domain.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5252Chloroplast Potential
Chain53 – 363311Ferredoxin--NADP reductase, chloroplastic
PRO_0000019410

Regions

Domain84 – 206123FAD-binding FR-type
Nucleotide binding142 – 1454FAD By similarity
Nucleotide binding163 – 1653FAD By similarity
Nucleotide binding180 – 1823FAD By similarity
Nucleotide binding253 – 2542NADP By similarity
Nucleotide binding283 – 2842NADP By similarity
Nucleotide binding322 – 3232NADP By similarity

Sites

Binding site1451NADP By similarity
Binding site1651NADP By similarity
Binding site1691FAD By similarity
Binding site2211FAD By similarity
Binding site2211NADP; via amide nitrogen By similarity
Binding site2931NADP By similarity
Binding site3611NADP By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P41346-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: CB0C8CC6D3203063

FASTA36340,579
        10         20         30         40         50         60 
MAAAVTAAVS LPYSNSTSLP IRTSIVAPER LVFKKVSLNS VSISGRVGTI RAQITTEAEA 

        70         80         90        100        110        120 
PVTKVVKHSK KQDEGIVVNK FKPKEPYVGR CLLNTKITGD DAPGETWHMV FTTEGEVPYR 

       130        140        150        160        170        180 
EGQSIGIVPD GIDKNGKPHK LRLYSIASSA IGDFGDSKTV SLCVKRLVYT NDAGEVVKGV 

       190        200        210        220        230        240 
CSNFLCDLKP GSEVKITGPV GKEMLMPKDP NATVIMLGTG TGIAPFRSFL WKMFFEKHED 

       250        260        270        280        290        300 
YKFNGLAWLF LGVPTSSSLL YKEEFEKMKE KAPENFRLDF AVSREQVNDK GEKMYIQTRM 

       310        320        330        340        350        360 
AQYAEELWEL LKKDNTFVYM CGLKGMEKGI DDIMVSIRPK DGIDWIEYKR TLKKAEQWNV 


EVY

« Hide

Hide | Top

References

[1]Lax A.R., Cary J.W.
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.

Hide | Top

Cross-references

Sequence databases

U14956 mRNA. Translation: AAA21758.1.

3D structure databases

HSSPHSSP built from PDB template 1QG0 based on UniProtKB P10933.
SMRP41346. Positions 55-362.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.18.1.2. 30.

Family and domain databases

InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012146. Frd-NADP+_RD.
IPR015701. FRD_Red.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]
PANTHERPTHR19384:SF1. FRD_Red. 1 hit.
PfamPF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSPR00371. FPNCR.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameFENR_VICFA
AccessionPrimary (citable) accession number: P41346
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents