Skip Header

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

Reviewed, UniProtKB/Swiss-Prot A0LT79 (FENR_ACIC1)

Last modified September 1, 2009. Version 25. 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

Hide | Top

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: Acel_0866
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Acidothermaceae › Acidothermus

Hide | Top

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

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.

Hide | Top

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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 325325Ferredoxin--NADP reductase HAMAP MF_01685
PRO_0000364779

Sites

Binding site281FAD By similarity
Binding site361FAD By similarity
Binding site411FAD By similarity
Binding site811FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1161FAD; via amide nitrogen By similarity
Binding site2751FAD By similarity
Binding site3161FAD By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
A0LT79-1 [UniParc].

Last modified March 3, 2009. Version 2.
Checksum: 974720C147D532C6

FASTA32534,930
        10         20         30         40         50         60 
MLIVGAGPAG LYAAYYAGFR AMSVVVLDSL TEPGGQLAAL YPEKVIYDVG GIPAILGREL 

        70         80         90        100        110        120 
AADLYKQAMT YNPVMLLGHG ADQLFRLDDG SFLVTTTTGL LIHAKAIIVT AGIGVFTPRR 

       130        140        150        160        170        180 
LPVGQEYEGR GLRYFVPNPQ ELAGKRILVV GGGDSAVDYA LMLEKVAASV TLIHRRHEFR 

       190        200        210        220        230        240 
AHEASVEQLR ASSVRILTPY QVSAVYGDDR VTAVDVTDHD TKHVERLDVD EIVAALGFVA 

       250        260        270        280        290        300 
ELGPLAEWGM ELRQRHIVVD TTMATSVPRI YAAGDIADYP GKVKLISVGF GEAAIAVNNA 

       310        320 
AVAIDPSKKL FPGHSSDPDR HPTER

« Hide

Hide | Top

References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
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., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Hide | Top

Cross-references

Sequence databases

CP000481 Genomic DNA. Translation: ABK52639.1. Different initiation.
RefSeqYP_872625.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0LT79.

Genome annotation databases

GeneID4485643.
GenomeReviewsGene locus Acel_0866 in contig CP000481_GR.
KEGGace:Acel_0866.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_01685.
[Tree]
InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR001327. Pyr_OxRdtase_NAD_bd.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
[Graphical view]
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...

Hide | Top

Entry information

Entry nameFENR_ACIC1
AccessionPrimary (citable) accession number: A0LT79
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: March 3, 2009
Last modified: September 1, 2009
This is version 25 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

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