Skip Header

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

A0LXL9 (FENR1_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 30. Feed History...

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

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:GFO_0125
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteria › Flavobacteriales › Flavobacteriaceae › Gramella

Protein attributes

Sequence length353 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)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFAD binding

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 – 353353Ferredoxin--NADP reductase 1 HAMAP MF_01685
PRO_0000364844

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
A0LXL9-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 2BF0BA0963DE66F9

FASTA35338,726
        10         20         30         40         50         60 
MIKTDILIIG AGPTGLFAVF EAGLLKLKCH LIDALPQPGG QCSEIYPKKP IYDIPGFPEV 

        70         80         90        100        110        120 
LAGDLVDNLM EQIKPFEPGF TLGERAETID KQEDGSFIVT TSQGAKHHAP VVVIAGGLGS 

       130        140        150        160        170        180 
FEPRKPPIPS IKEYENKGVA YIIRDPEVYR DKKVVIAGGG DSALDWSIFL ADVASEVSLV 

       190        200        210        220        230        240 
HRRKDFRGAL DSVEKVEELS KIGKINLITD AEVVDLKGEN ELDSVLIRHR DQARGEELKD 

       250        260        270        280        290        300 
TDHFIPLFGL SPKLGPIANW GLEIEKNAIK VDNAYDYQTN IPGIYAIGDV NTYKGKLKLI 

       310        320        330        340        350 
LCGFHEAAIM CQSAYQRINP DKKYVMKYTT VSGVSGFDGS KKEAKKEVVK SIN

« 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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU207366 Genomic DNA. Translation: CAL65114.1.
RefSeqYP_860192.1.

3D structure databases

ProteinModelPortalA0LXL9.
SMRA0LXL9. Positions 3-332.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0LXL9.

Genome annotation databases

GeneID4649663.
GenomeReviewsGene locus GFO_0125 in contig CU207366_GR.
KEGGgfo:GFO_0125.
NMPDRfig|411154.5.peg.123.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0492.
HOGENOMHBG669726.
OMAFQVFELG.
ProtClustDBCLSK851229.

Enzyme and pathway databases

BioCycGFOR411154:GFO_0125-MONOMER.

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...

Entry information

Entry nameFENR1_GRAFK
AccessionPrimary (citable) accession number: A0LXL9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: December 12, 2006
Last modified: August 10, 2010
This is version 30 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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents