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Reviewed, UniProtKB/Swiss-Prot A5FYH8 (FENR_ACICJ)

Last modified November 3, 2009. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

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Names and origin

Protein namesRecommended name:
    Ferredoxin--NADP reductase
      Short name=Fd-NADP+ reductase
      Short name=FNR
    EC=1.18.1.2
Gene names
Ordered Locus Names: Acry_1452
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Acidiphilium

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Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH. HAMAP MF_01685

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the ferredoxin--NADP reductase type 2 family.

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Ontologies

Keywords
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFAD binding

Inferred from electronic annotation. Source: HAMAP

NADP or NADPH binding

Inferred from electronic annotation. Source: HAMAP

ferredoxin-NADP+ reductase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Ferredoxin--NADP reductase HAMAP MF_01685
PRO_0000364778

Sites

Binding site361FAD By similarity
Binding site441FAD By similarity
Binding site491FAD By similarity
Binding site891FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1231FAD; via amide nitrogen By similarity
Binding site2901FAD By similarity
Binding site3311FAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
A5FYH8-1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 15A3EFF850C35C0D

FASTA33935,089
        10         20         30         40         50         60 
MAETITTDVA IIGAGPAGLF AVFECGMLKL GTVLIDALGE VGGQCAALYP EKPIYDIPAL 

        70         80         90        100        110        120 
PAIEAAGLIE NLERQIAPFA APRLLGRLVT AISGSSGDFT IGTDLGDIVR AKAIIIAAGA 

       130        140        150        160        170        180 
GAFGPNRPPL EGLAAYEASG AVQYYVKRRE ALRGKRVVIA GGGDSAVDWA LALCGIASSI 

       190        200        210        220        230        240 
AVVHRRPKFR AAPESAAQLA EAAARGDIDL VIPYQLHALH GADGALRTVE VADLDGATRH 

       250        260        270        280        290        300 
LEADVLLPFF GLATDLGPVA TWGLELSLHH VLVTPSTCET STRGIFAIGD VAQYPGKLKL 

       310        320        330 
ILQGFSEAAM AAHAIHPIVH PDEALHFEYS TSKGVPGTA

« Hide

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References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000697 Genomic DNA. Translation: ABQ30660.1.
RefSeqYP_001234579.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5FYH8.

Genome annotation databases

GeneID5161852.
GenomeReviewsGene locus Acry_1452 in contig CP000697_GR.
KEGGacr:Acry_1452.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMADWALMLE.

Family and domain databases

HAMAPMF_01685.
[Tree]
InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR016040. NAD(P)-bd_dom.
IPR001327. Pyr_OxRdtase_NAD_bd.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00469. PNDRDTASEII.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

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Entry information

Entry nameFENR_ACICJ
AccessionPrimary (citable) accession number: A5FYH8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: June 12, 2007
Last modified: November 3, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

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