Skip Header

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

B3R4A7 (FENR1_CUPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferredoxin--NADP reductase 1
Short name=FNR 1
Short name=Fd-NADP+ reductase 1
EC=1.18.1.2
Gene names
Ordered Locus Names:RALTA_A1176
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Ontologies

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

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360Ferredoxin--NADP reductase 1 HAMAP MF_01685
PRO_0000364825

Sites

Binding site431FAD By similarity
Binding site511FAD By similarity
Binding site561FAD By similarity
Binding site961FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1411FAD; via amide nitrogen By similarity
Binding site3071FAD By similarity
Binding site3481FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B3R4A7 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 903CABEA8F247362

FASTA36038,150
        10         20         30         40         50         60 
MPTATPATAP VTTTDVLIVG AGPVGLFAAF QAGVLGLKCE LIDVLDRAGG QCTELYPEKP 

        70         80         90        100        110        120 
IYDIPAVPGC LAQDLVDRLL EQCAPFDFPM HFGQRAESVA EIPAPAASAG HAGHERLLVT 

       130        140        150        160        170        180 
TDGGKRFDVA AVLICAGAGA FAPQRVSLPE AAALEGRHVH YAVRDVSHFA GKRVIVAGGG 

       190        200        210        220        230        240 
DSALDWALAL RKVAARVTLL HRREGFRAAD GTVAEMRRAV AEGEMDFVVG MLGALRTEGA 

       250        260        270        280        290        300 
DGGLSEVEVR TRDGSTVLPA EELVALYGLV SEPGPIAQWD LDMRAGRILV DTTTYESSRR 

       310        320        330        340        350        360 
GIFAAGDIAF YPNKQKLILS GFHEAALALR KAYHYAFPEK ALVHVHTSNN AALKEKLTHA

« Hide

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].
Strain: R1 / LMG 19424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU633749 Genomic DNA. Translation: CAQ69140.1.
RefSeqYP_002005207.1. NC_010528.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB3R4A7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6452936.
GenomeReviewsGene locus RALTA_A1176 in contig CU633749_GR.
KEGGcti:RALTA_A1176.
PATRIC21528944. VBICupTai42494_1149.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG669726.
OMAYPNKQKL.
ProtClustDBCLSK896839.

Family and domain databases

HAMAPMF_01685. FENR2.
[Tree]
InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR022890. Fd--NADP_Rdtase_type_2.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
KOK00384.
PANTHERPTHR22912:SF53. PTHR22912:SF53. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProtoNetSearch...

Entry information

Entry nameFENR1_CUPTR
AccessionPrimary (citable) accession number: B3R4A7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: September 2, 2008
Last modified: January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents