Skip Header

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

A0LY71 (FENR2_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 43. 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:GFO_0330
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Gramella

Protein attributes

Sequence length354 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 – 354354Ferredoxin--NADP reductase 2 HAMAP MF_01685
PRO_0000364845

Sites

Binding site141FAD By similarity
Binding site331FAD By similarity
Binding site411FAD By similarity
Binding site461FAD By similarity
Binding site861FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1211FAD; via amide nitrogen By similarity
Binding site2891FAD By similarity
Binding site3301FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A0LY71 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: F3720749E124E7F9

FASTA35438,808
        10         20         30         40         50         60 
MIKTDILIIG AGPTGLFTVF EAGLLKLKTH LIDALPQPGG QCSEIYPKKP IYDIPAFPEI 

        70         80         90        100        110        120 
LAGDLVSNLM EQIRPFKPGF TLGERAETLE KLDDGSFIVT TNKGTQHHAP VVAIAGGLGS 

       130        140        150        160        170        180 
FEPRKPPIPN IADFEDKGVS YFIKDPEVYR DKKVVIAGGG DSALDWAIYL ADVASEVALV 

       190        200        210        220        230        240 
HRRAEFRGAL DSVERVSELA KLGRIEMITN AEVVGLRGED NLEQVVIRHK DKARGEEFRD 

       250        260        270        280        290        300 
VDDFIPLFGL SPKLGPIGSW GLEIERNAIK VDNSYDYQTN IPGVYAIGDV NTYKGKLKLI 

       310        320        330        340        350 
LSGFHEAAIM CQSAYQRIYP DKKYVLKYTT VGGVEGFDGT KKEAKKEVVQ SIGV

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT0803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU207366 Genomic DNA. Translation: CAL65316.1.
RefSeqYP_860384.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0LY71.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0LY71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4651367.
GenomeReviewsGene locus GFO_0330 in contig CU207366_GR.
KEGGgfo:GFO_0330.
NMPDRfig|411154.5.peg.311.
PATRIC22069531. VBIGraFor5527_0324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0492.
HOGENOMHBG669726.
OMAHEVALMA.
ProtClustDBCLSK851229.

Enzyme and pathway databases

BioCycGFOR411154:GFO_0330-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_GRAFK
AccessionPrimary (citable) accession number: A0LY71
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 43 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