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P21890 (FENR_NOSSO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferredoxin--NADP reductase

Short name=FNR
EC=1.18.1.2
Gene names
Name:petH
OrganismNostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.)
Taxonomic identifier1168 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

FAD.

Subcellular location

Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note: May be bound to the thylakoid membrane or anchored to the thylakoid-bound phycobilisomes.

Sequence similarities

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

Contains 1 cpcD-like domain.

Contains 1 FAD-binding FR-type domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Ferredoxin--NADP reductase
PRO_0000167632

Regions

Domain17 – 7559CpcD-like
Domain155 – 279125FAD-binding FR-type
Nucleotide binding214 – 2174FAD
Nucleotide binding235 – 2373FAD
Nucleotide binding253 – 2553FAD
Nucleotide binding330 – 3312NADP By similarity
Nucleotide binding360 – 3612NADP
Nucleotide binding370 – 3745NADP
Nucleotide binding399 – 4002NADP By similarity

Sites

Binding site2171NADP By similarity
Binding site2371NADP
Binding site2411FAD
Binding site2941FAD
Binding site2941NADP; via amide nitrogen
Binding site4381NADP By similarity

Experimental info

Sequence conflict1801I → L AA sequence Ref.3

Secondary structure

................................................................ 440
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21890 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 8E1F61D0F09338B6

FASTA44048,865
        10         20         30         40         50         60 
MSNQGAFDGA ANVESGSRVF VYEVVGMRQN EETDQTNYPI RKSGSVFIRV PYNRMNQEMQ 

        70         80         90        100        110        120 
RITRLGGKIV TIQTVSALQQ LNGRTTIATV TDASSEIAKS EGNGKATPVK TDSGAKAFAK 

       130        140        150        160        170        180 
PPAEEQLKKK DNKGNTMTQA KAKHADVPVN LYRPNAPFIG KVISNEPLVK EGGIGIVQHI 

       190        200        210        220        230        240 
KFDLTGGNLK YIEGQSIGII PPGVDKNGKP EKLRLYSIAS TRHGDDVDDK TISLCVRQLE 

       250        260        270        280        290        300 
YKHPESGETV YGVCSTYLTH IEPGSEVKIT GPVGKEMLLP DDPEANVIML ATGTGIAPMR 

       310        320        330        340        350        360 
TYLWRMFKDA ERAANPEYQF KGFSWLVFGV PTTPNILYKE ELEEIQQKYP DNFRLTYAIS 

       370        380        390        400        410        420 
REQKNPQGGR MYIQDRVAEH ADELWQLIKN QKTHTYICGL RGMEEGIDAA LSAAAAKEGV 

       430        440 
TWSDYQKDLK KAGRWHVETY 

« Hide

References

[1]"Homology of the N-terminal domain of the petH gene product from Anabaena sp. PCC 7119 to the CpcD phycobilisome linker polypeptide."
Fillat M.F., Flores E., Gomez-Moreno C.
Plant Mol. Biol. 22:725-729(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence of the ferredoxin-NADP(+)-reductase gene from Anabaena PCC 7119."
Fillat M.F., Bakker H.A.C., Weisbeek P.J.
Nucleic Acids Res. 18:7161-7161(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-440.
[3]"Purification and properties of ferredoxin-NADP+ oxidoreductase from the nitrogen-fixing cyanobacteria Anabaena variabilis."
Sancho J., Peleato M.L., Gomez-Moreno C., Edmondson D.E.
Arch. Biochem. Biophys. 260:200-207(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 152-183.
Strain: 1403.46.
[4]"X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8-A resolution, and crystallographic studies of NADP+ binding at 2.25-A resolution."
Serre L., Vellieux F.M.D., Medina M., Gomez-Moreno C., Fontecilla-Camps J.-C., Frey M.
J. Mol. Biol. 263:20-39(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 137-440.
[5]"Role of Arg100 and Arg264 from Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal NADP+ binding and electron transfer."
Martinez-Julvez M., Hermoso J., Hurley J.K., Mayoral T., Sanz-Aparicio J., Tollin G., Gomez-Moreno C., Medina M.
Biochemistry 37:17680-17691(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 146-440.
[6]"Structural basis of the catalytic role of Glu301 in Anabaena PCC 7119 ferredoxin-NADP+ reductase revealed by X-ray crystallography."
Mayoral T., Medina M., Sanz-Aparicio J., Gomez-Moreno C., Hermoso J.A.
Proteins 38:60-69(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 137-440.
[7]"Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin molecule."
Morales R., Kachalova G., Vellieux F., Charon M.-H., Frey M.
Acta Crystallogr. D 56:1408-1412(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72394 Genomic DNA. Translation: CAA51088.1.
X54039 Genomic DNA. Translation: CAA37973.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B2RX-ray1.80A137-440[»]
1BJKX-ray2.30A146-440[»]
1BQEX-ray2.45A146-440[»]
1E62X-ray2.30A137-440[»]
1E63X-ray2.30A137-440[»]
1E64X-ray2.30A137-440[»]
1EWYX-ray2.38A/B138-440[»]
1GJRX-ray2.10A137-440[»]
1GO2X-ray1.70A137-440[»]
1GR1X-ray2.50A138-440[»]
1H42X-ray2.15A137-440[»]
1H85X-ray2.30A146-440[»]
1OGIX-ray1.64A138-440[»]
1OGJX-ray1.64A138-440[»]
1QGYX-ray1.70A146-440[»]
1QGZX-ray2.30A146-440[»]
1QH0X-ray1.93A146-440[»]
1QUEX-ray1.80A138-440[»]
1QUFX-ray2.25A137-440[»]
1W34X-ray1.73A137-440[»]
1W35X-ray1.90A137-440[»]
1W87X-ray3.00A/B137-440[»]
2BMWX-ray1.50A137-440[»]
2BSAX-ray1.92A138-440[»]
2VYQX-ray1.90A137-440[»]
2VZLX-ray1.93A137-440[»]
2X3UX-ray1.93A138-440[»]
3ZBTX-ray1.92A138-440[»]
3ZBUX-ray1.89A138-440[»]
3ZC3X-ray2.30A/B138-440[»]
4BPRX-ray2.00A138-440[»]
4C43X-ray1.70A138-440[»]
ProteinModelPortalP21890.
SMRP21890. Positions 138-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP21890. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008213. CpcD-like_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015701. FNR.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF01383. CpcD. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSPR00371. FPNCR.
SMARTSM01094. CpcD. 1 hit.
[Graphical view]
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51441. CPCD_LIKE. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21890.

Entry information

Entry nameFENR_NOSSO
AccessionPrimary (citable) accession number: P21890
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references