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Q44532 (FENR_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ferredoxin--NADP reductase
Short name=FNR
Short name=Protein X
EC=1.18.1.2
Gene names
Name:fpr
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Ontologies

Keywords
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Molecular functionferredoxin-NADP+ reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 258257Ferredoxin--NADP reductase
PRO_0000167639

Regions

Domain2 – 102101FAD-binding FR-type
Nucleotide binding51 – 544FAD
Nucleotide binding67 – 693FAD
Nucleotide binding74 – 774FAD
Nucleotide binding144 – 1452NADP By similarity
Nucleotide binding181 – 1822NADP By similarity
Nucleotide binding220 – 2212NADP By similarity
Nucleotide binding254 – 2585FAD

Sites

Binding site541NADP By similarity
Binding site1171FAD
Binding site1171NADP; via amide nitrogen By similarity
Binding site2521NADP By similarity

Secondary structure

1 ............................................... 258
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q44532 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2865C2FC786A6C04

FASTA25829,417
        10         20         30         40         50         60 
MSNLNVERVL SVHHWNDTLF SFKTTRNPSL RFENGQFVMI GLEVDGRPLM RAYSIASPNY 

        70         80         90        100        110        120 
EEHLEFFSIK VQNGPLTSRL QHLKEGDELM VSRKPTGTLV TSDLLPGKHL YMLSTGTGLA 

       130        140        150        160        170        180 
PFMSLIQDPE VYERFEKVVL IHGVRQVNEL AYQQFITEHL PQSEYFGEAV KEKLIYYPTV 

       190        200        210        220        230        240 
TRESFHNQGR LTDLMRSGKL FEDIGLPPIN PQDDRAMICG SPSMLDESCE VLDGFGLKIS 

       250 
PRMGEPGDYL IERAFVEK

« Hide

References

[1]"Azotobacter vinelandii NADPH:ferredoxin reductase cloning, sequencing, and overexpression."
Isas J.M., Yannone S.M., Burgess B.K.
J. Biol. Chem. 270:21258-21263(1995) [PubMed: 7673160] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW.
[2]"Purification and characterization of a NADP+/NADPH-specific flavoprotein that is overexpressed in FdI-strains of Azotobacter vinelandii."
Isas J.M., Burgess B.K.
J. Biol. Chem. 269:19404-19409(1994) [PubMed: 8034707] [Abstract]
Cited for: CHARACTERIZATION.
Strain: ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW.
[3]"The crystal structure of NADPH:ferredoxin reductase from Azotobacter vinelandii."
Prasad G.S., Kresge N., Muhlberg A.B., Shaw A., Jung Y.S., Burgess B.K., Stout C.D.
Protein Sci. 7:2541-2549(1998) [PubMed: 9865948] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FAD.
Strain: LM100.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L36319 Genomic DNA. Translation: AAA83029.1.
PIRA57432.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8PX-ray2.00A1-258[»]
ProteinModelPortalQ44532.
SMRQ44532. Positions 2-258.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00371. FPNCR.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFENR_AZOVI
AccessionPrimary (citable) accession number: Q44532
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: June 28, 2011
This is version 71 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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