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Q65GY3 (FENR1_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. 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

Names and origin

Protein namesRecommended name:
Ferredoxin--NADP reductase 1

Short name=FNR 1
Short name=Fd-NADP+ reductase 1
EC=1.18.1.2
Gene names
Ordered Locus Names:BLi02810, BL02042
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length349 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349Ferredoxin--NADP reductase 1 HAMAP MF_01685
PRO_0000364797

Sites

Binding site361FAD By similarity
Binding site441FAD By similarity
Binding site481FAD By similarity
Binding site881FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1231FAD; via amide nitrogen By similarity
Binding site2901FAD By similarity
Binding site3311FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65GY3 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 7360705E89C0111A

FASTA34938,342
        10         20         30         40         50         60 
MSRNELFDVT VIGGGPAGLY SAFYSGLRGM KAKIIEYQPM LGGKVHVYPE KMIWDVGGLT 

        70         80         90        100        110        120 
PISGAKLIEQ LVQQGLTFHP EVLLNEKVES IARNEEGLFE LHTAASGVHL SKTVIVAVGG 

       130        140        150        160        170        180 
GILNPQKLQI EGAERFEVSN LNYTVKSLQH FKDKTVIVSG GGNSAVDWAN ELEPVAKKVY 

       190        200        210        220        230        240 
LAYRKDALSG HEAQVDQLLN SSVSCFFHTE ITKLIASEDH EVIERVELTN AQTGEVMELP 

       250        260        270        280        290        300 
VDEVVINHGY ERDTSLLENS RLDVTRVDDY YIAGTSNCQS SVPGLYAAGD IVHYEGKLHL 

       310        320        330        340 
IAGAFQDAAN AVNSAKRFID PEAHKSAMVS SHNEVFKERN RELVKKMFV 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU24315.1.
AE017333 Genomic DNA. Translation: AAU41681.1.
RefSeqYP_079953.1. NC_006270.3.
YP_092374.1. NC_006322.1.

3D structure databases

ProteinModelPortalQ65GY3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65GY3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000058018; EBBACP00000056549; EBBACG00000058009.
EBBACT00000058693; EBBACP00000057126; EBBACG00000058684.
GeneID3028262.
3097980.
GenomeReviewsGene locus BLi02810 in contig AE017333_GR.
Gene locus BL02042 in contig CP000002_GR.
KEGGbld:BLi02810.
bli:BL02042.
NMPDRfig|279010.5.peg.3102.
PATRIC18951320. VBIBacLic203714_2861.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0492.
GeneTreeEBGT00050000000432.
HOGENOMHBG669726.
OMAFNTSITK.
ProtClustDBCLSK904552.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI02810-MONOMER.
BLIC279010:BL02042-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.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
[Graphical view]
KOK00384.
PANTHERPTHR22912:SF53. PTHR22912:SF53. 1 hit.
PfamPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00469. PNDRDTASEII.
ProtoNetSearch...

Entry information

Entry nameFENR1_BACLD
AccessionPrimary (citable) accession number: Q65GY3
Secondary accession number(s): Q62SE4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 59 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