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Reviewed, UniProtKB/Swiss-Prot B3R5L8 (FENR2_CUPTR)

Last modified November 3, 2009. Version 12. 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 2
      Short name=Fd-NADP+ reductase 2
      Short name=FNR 2
    EC=1.18.1.2
Gene names
Ordered Locus Names: RALTA_A2094
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

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Protein attributes

Sequence length369 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 – 369369Ferredoxin--NADP reductase 2 HAMAP MF_01685
PRO_0000364826

Sites

Binding site581FAD By similarity
Binding site661FAD By similarity
Binding site711FAD By similarity
Binding site1111FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1461FAD; via amide nitrogen By similarity
Binding site3111FAD By similarity
Binding site3521FAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
B3R5L8-1 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 3BF4AC9066EAB7E1

FASTA36940,311
        10         20         30         40         50         60 
MDLSIPNPVA DATRQVEGGS PAGGQPLEID ALIVGAGPVG LFQVFELGLL EIKAHVIDSL 

        70         80         90        100        110        120 
KVVGGQCVEL YPDKPIYDIP AVPSCTGQEL TDNLLKQIEP FEPTFHLGQE VSVVERRDDG 

       130        140        150        160        170        180 
RFFVETSLGT RFITKTIFIA AGVGSFQPRT LKVDGIDKFD GKQLFYRVKD PSRFHGRNLV 

       190        200        210        220        230        240 
IVGGGDSALD WTLDLVGKAE SVVMIHRRDG FRAAPASVAK MKELCEQMEM QFLVGQISGY 

       250        260        270        280        290        300 
EEKDGVLTEI KVSGADGVTR RLPLDDLLVF FGLSPKLGPI AEWGLDLERK QIKVDTEKFQ 

       310        320        330        340        350        360 
TNIPGIFAVG DINTYPGKKK LILSGFHEAA LAAFGAAPYI FPEKKIHMQY TTTSPKLHKV 


LGVESPVFD

« Hide

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References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CU633749 Genomic DNA. Translation: CAQ70031.1.
RefSeqYP_002006094.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6453523.
GenomeReviewsGene locus RALTA_A2094 in contig CU633749_GR.
KEGGcti:RALTA_A2094.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMADWALMLE.

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.
ProtoNetSearch...

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Entry information

Entry nameFENR2_CUPTR
AccessionPrimary (citable) accession number: B3R5L8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: September 2, 2008
Last modified: November 3, 2009
This is version 12 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