Skip Header

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

Q0K8J6 (FENR2_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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 2
Short name=FNR 2
Short name=Fd-NADP+ reductase 2
EC=1.18.1.2
Gene names
Ordered Locus Names:H16_A2592
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length369 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 – 369369Ferredoxin--NADP reductase 2 HAMAP MF_01685
PRO_0000364904

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

Sequences

Sequence LengthMass (Da)Tools
Q0K8J6 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: F6398C2ECCC01733

FASTA36940,324
        10         20         30         40         50         60 
MDLSIPNPVA DTTKQVDGGS PAGGQPQEID ALIVGAGPVG LFQVFELGLL EIKAHVIDSL 

        70         80         90        100        110        120 
KVVGGQCVEL YPDKPIYDIP AVPICTGQEL TDNLLKQIEP FEPTFHLGQE VAVVERREDG 

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

       190        200        210        220        230        240 
IIGGGDSALD WTLDLVGKAE SVVMIHRRDG FRAAPASVAK MKELCEQMEM QFLVGQVGGY 

       250        260        270        280        290        300 
EEKDGVLTEI KVTGADGVTR RLPVDDLLVF FGLSPKLGPI AEWGLDLERK QIKVDTEKFE 

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


LGVDSPVFD

« Hide

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].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM260479 Genomic DNA. Translation: CAJ93675.1.
RefSeqYP_727043.1. NC_008313.1.

3D structure databases

ProteinModelPortalQ0K8J6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0K8J6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4249001.
GenomeReviewsGene locus H16_A2592 in contig AM260479_GR.
KEGGreh:H16_A2592.
PATRIC35234689. VBIRalEut6770_2979.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0492.
HOGENOMHBG669726.
OMAFQVFELG.
ProtClustDBCLSK939521.

Enzyme and pathway databases

BioCycREUT381666:H16_A2592-MONOMER.

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.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
[Graphical view]
KOK00384.
PANTHERPTHR22912:SF53. PTHR22912:SF53. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00469. PNDRDTASEII.
ProtoNetSearch...

Entry information

Entry nameFENR2_CUPNH
AccessionPrimary (citable) accession number: Q0K8J6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 3, 2006
Last modified: January 25, 2012
This is version 42 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