Skip Header

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

Reviewed, UniProtKB/Swiss-Prot Q9Z615 (FENR_BUCAP)

Last modified November 3, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Ferredoxin--NADP reductase
      Short name=FNR
    EC=1.18.1.2
Alternative name(s):
    Flavodoxin reductase
      Short name=FLXR
      Short name=FLDR
Gene names
Name: fpr
Ordered Locus Names: BUsg_560
OrganismBuchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]
Taxonomic identifier98794 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Transports electrons between flavodoxin or ferredoxin and NADPH By similarity.

Catalytic activity

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

Cofactor

FAD By similarity.

Sequence similarities

Belongs to the ferredoxin--NADP reductase type 1 family.

Contains 1 FAD-binding FR-type domain.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

ferredoxin-NADP+ reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257Ferredoxin--NADP reductase
PRO_0000167641

Regions

Domain2 – 110109FAD-binding FR-type
Nucleotide binding59 – 624FAD By similarity
Nucleotide binding82 – 854FAD By similarity
Nucleotide binding152 – 1532NADP By similarity
Nucleotide binding182 – 1832NADP By similarity
Nucleotide binding222 – 2232NADP By similarity

Sites

Binding site621NADP By similarity
Binding site1251FAD By similarity
Binding site1251NADP; via amide nitrogen By similarity
Binding site2541NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z615-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: F1BF24F2D5FAA07B

FASTA25730,079
        10         20         30         40         50         60 
MNPWINANVL KVHKWTQNLF SLILNAEIAP FQAGQFTKLA LNEENINFSN NVKKKKIQRA 

        70         80         90        100        110        120 
YSFVNAPSNK NLEIYIVRIL NGKLSNLLYN LKSGDNLFIK EKSFGFFTLD EIPNCKTLWM 

       130        140        150        160        170        180 
FATGTGIGPY CSILQEYKNI NRFKNIILIH AVRYQNELTY LPLMKQLYKS YNGKLKIETI 

       190        200        210        220        230        240 
VSREKNHNSL YGRIPLLLQN QILEKKIGLK INRNDSHVML CGNPAMVKDT YLFLQKDRCM 

       250 
QKNLRRKHGH ITMENYW 

« Hide

References

« Hide 'large scale' references
[1]"Buchnera plasmid-associated trpEG probably originated from a chromosomal location between hslU and fpr."
Clark M.A., Baumann P., Moran M.A.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AF108665 Genomic DNA. Translation: AAD19635.1.
AE013218 Genomic DNA. Translation: AAM68098.1.
RefSeqNP_660887.1.

3D structure databases

HSSPHSSP built from PDB template 1FDR based on UniProtKB P28861.
ModBaseSearch...

Genome annotation databases

GeneID1005631.
GenomeReviewsGene locus BUsg_560 in contig AE013218_GR.
KEGGbas:BUsg560.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9Z615.
OMAIMLCGNP.

Enzyme and pathway databases

BioCycBAPH198804:BUSG560-MON.

Family and domain databases

InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]
PfamPF00175. NAD_binding_1. 1 hit.
[Graphical view]
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFENR_BUCAP
AccessionPrimary (citable) accession number: Q9Z615
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: November 3, 2009
This is version 61 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)

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

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