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A5VM22 (FENR_LACRD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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

Short name=FNR
Short name=Fd-NADP(+) reductase
EC=1.18.1.2
Gene names
Ordered Locus Names:Lreu_1657
OrganismLactobacillus reuteri (strain DSM 20016) [Complete proteome] [HAMAP]
Taxonomic identifier557436 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH. HAMAP-Rule MF_01685

Cofactor

Binds 1 FAD per subunit By similarity. HAMAP-Rule MF_01685

Subunit structure

Homodimer By similarity. HAMAP-Rule 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_functionNADP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

ferredoxin-NADP+ reductase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Ferredoxin--NADP reductase HAMAP-Rule MF_01685
PRO_0000364858

Sites

Binding site351FAD By similarity
Binding site431FAD By similarity
Binding site481FAD By similarity
Binding site881FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1221FAD; via amide nitrogen By similarity
Binding site2861FAD By similarity
Binding site3261FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A5VM22 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 6F0FFA8D88192A71

FASTA33235,792
        10         20         30         40         50         60 
MAEKIYDVTI IGGGPAGMFA SFYCGLHELD AQLIESLPQL GGQVGALYPE KQVWDVAGMP 

        70         80         90        100        110        120 
GVTGHDLIAK LEEQMAVAPI DQFLGETVED VIKGDDGTFT IKSAKRVSRS RAVIIALGNG 

       130        140        150        160        170        180 
AFTPRKLALE GAAEIEGKQL SYFVNHKADY ADKRVAILGG GDSAIDIALM LEPVAKEVHL 

       190        200        210        220        230        240 
VHRRDQFRGL EHTVTQLKQS SVQLDTPFLP RALTVEDDET VTLDLKKMRS DDEAQLNVDK 

       250        260        270        280        290        300 
IVVNYGFTSN NAALNQWSLD LAAEHNLIKV DSMMETSTEG VYAIGDGVTY PGKVALIAAG 

       310        320        330 
FGEAPTAVTA LAKKLYPDKR MAMHSSSMGI TK 

« Hide

References

[1]"The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri."
Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M., Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M., Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L. expand/collapse author list , Ivanova N., Kyrpides N.C., Walter J.
PLoS Genet. 7:E1001314-E1001314(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 20016.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000705 Genomic DNA. Translation: ABQ83896.1.
RefSeqYP_001272233.1. NC_009513.1.

3D structure databases

ProteinModelPortalA5VM22.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557436.Lreu_1657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ83896; ABQ83896; Lreu_1657.
GeneID5189025.
KEGGlre:Lreu_1657.
PATRIC22256575. VBILacReu87937_1675.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0492.
HOGENOMHOG000072909.
KOK00384.
OMATHYSKTV.
OrthoDBEOG661H9M.
ProtClustDBCLSK2326607.

Enzyme and pathway databases

BioCycLREU557436:GC7Y-1740-MONOMER.

Family and domain databases

HAMAPMF_01685. FENR2.
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]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00469. PNDRDTASEII.
ProtoNetSearch...

Entry information

Entry nameFENR_LACRD
AccessionPrimary (citable) accession number: A5VM22
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 58 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