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Reviewed, UniProtKB/Swiss-Prot Q0KCD1 (FENR1_RALEH)

Last modified January 19, 2010. Version 31. 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 1
      Short name=Fd-NADP+ reductase 1
      Short name=FNR 1
    EC=1.18.1.2
Gene names
Ordered Locus Names: H16_A1199
OrganismRalstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

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Protein attributes

Sequence length361 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 – 361361Ferredoxin--NADP reductase 1 HAMAP MF_01685
PRO_0000364903

Sites

Binding site441FAD By similarity
Binding site521FAD By similarity
Binding site571FAD By similarity
Binding site971FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1421FAD; via amide nitrogen By similarity
Binding site3081FAD By similarity
Binding site3491FAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q0KCD1-1 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 334B3D7E76D76CB0

FASTA36138,628
        10         20         30         40         50         60 
MSTATPLAPT PVTTTDVLIV GAGPVGLFAA FQAGVLGLRC ELIDVLDRAG GQCTELYPEK 

        70         80         90        100        110        120 
PIYDIPAVPG CLAQDLVDRL LEQCAPFAFP MHFGQRAESL SEIPRQPAPD GHAAHERLLV 

       130        140        150        160        170        180 
TTDGGKRFDV SAVLICAGAG AFAPQRVSLP EAPALEGRHV HYAVRDVSRF AGKRVVVAGG 

       190        200        210        220        230        240 
GDSALDWALA LRKVAARVTL LHRREGFRAA DGTVAEMREA VAAGEMDFVV GMLGALRTEG 

       250        260        270        280        290        300 
QDGPLTEVEV RTRDGSTVLP ADELVALYGL VSEPGPIAQW DMDMRAGRIL VDTTTYESSR 

       310        320        330        340        350        360 
RGIFAAGDIA YYTNKQKLIL SGFHEAALAL RRAYHYAFPE KALVHVHTSN NAALKEKLTH 


A

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References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM260479 Genomic DNA. Translation: CAJ92340.1.
RefSeqYP_725708.1.

3D structure databases

SMRQ0KCD1. Positions 13-354.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0KCD1.

Genome annotation databases

GeneID4249000.
GenomeReviewsGene locus H16_A1199 in contig AM260479_GR.
KEGGreh:H16_A1199.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0492.
HOGENOMHBG669726.
OMAYPNKQKL.

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 nameFENR1_RALEH
AccessionPrimary (citable) accession number: Q0KCD1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 3, 2006
Last modified: January 19, 2010
This is version 31 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