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Reviewed, UniProtKB/Swiss-Prot Q816D9 (FENR_BACCR)

Last modified January 19, 2010. Version 47. 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: BC_4926
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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Protein attributes

Sequence length331 AA.
Sequence statusComplete.
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. HAMAP MF_01685

Subunit structure

Homodimer By similarity. HAMAP MF_01685

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 – 331331Ferredoxin--NADP reductase HAMAP MF_01685
PRO_0000364790

Sites

Binding site201FAD By similarity
Binding site391FAD By similarity
Binding site471FAD By similarity
Binding site521FAD By similarity
Binding site921FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1261FAD; via amide nitrogen By similarity
Binding site2871FAD By similarity
Binding site3281FAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q816D9-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3D910538F9E38649

FASTA33136,748
        10         20         30         40         50         60 
MKVAENQKVY DITIIGGGPT GLFTAFYGGM RQASVKIIES LPQLGGQLSA LYPEKYIYDV 

        70         80         90        100        110        120 
AGFPKVRAQE LVDNLKEQMK KFDPTVCLEE AVDTLEKQAD GIFKLVTNKQ THYSKSVIIT 

       130        140        150        160        170        180 
AGNGAFQPRR LELEGTAKYE KKNLHYFVDD MNKFAGKRVV VFGGGDSAVD WTMMLEPIAE 

       190        200        210        220        230        240 
KVTIVHRRDK FRAHEHSVEN LMNSRAEVST PYVPVELIGD DKIEQVVLQH VKTEEKVIID 

       250        260        270        280        290        300 
VDDVIVNYGF VSSLGPIKNW GLDIQKNSIL VNSKMETNIP GIYAAGDICT YEGKVKLIAC 

       310        320        330 
GFGEAPTAVN NAKAYFDPNA KLQPMHSSSM F

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References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016877 Genomic DNA. Translation: AAP11799.1.
RefSeqNP_834598.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ816D9.

Genome annotation databases

GeneID1207268.
GenomeReviewsGene locus BC_4926 in contig AE016877_GR.
KEGGbce:BC4926.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0492.
HOGENOMHBG669726.
OMAIYLVHRR.

Enzyme and pathway databases

BioCycBCER226900:BC_4926-MONOMER.

Family and domain databases

HAMAPMF_01685. FENR2.
[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.
ProtoNetSearch...

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Entry information

Entry nameFENR_BACCR
AccessionPrimary (citable) accession number: Q816D9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: June 1, 2003
Last modified: January 19, 2010
This is version 47 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