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A5VM22

- FENR_LACRD

UniProt

A5VM22 - FENR_LACRD

Protein

Ferredoxin--NADP reductase

Gene

Lreu_1657

Organism
Lactobacillus reuteri (strain DSM 20016)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (10 Jul 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.UniRule annotation

    Cofactori

    Binds 1 FAD per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei35 – 351FADUniRule annotation
    Binding sitei43 – 431FADUniRule annotation
    Binding sitei48 – 481FADUniRule annotation
    Binding sitei88 – 881FAD; via amide nitrogen and carbonyl oxygenUniRule annotation
    Binding sitei122 – 1221FAD; via amide nitrogenUniRule annotation
    Binding sitei286 – 2861FADUniRule annotation
    Binding sitei326 – 3261FADUniRule annotation

    GO - Molecular functioni

    1. ferredoxin-NADP+ reductase activity Source: UniProtKB-HAMAP
    2. flavin adenine dinucleotide binding Source: UniProtKB-HAMAP
    3. NADP binding Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciLREU557436:GC7Y-1740-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferredoxin--NADP reductaseUniRule annotation (EC:1.18.1.2UniRule annotation)
    Short name:
    FNRUniRule annotation
    Short name:
    Fd-NADP(+) reductaseUniRule annotation
    Gene namesi
    Ordered Locus Names:Lreu_1657
    OrganismiLactobacillus reuteri (strain DSM 20016)
    Taxonomic identifieri557436 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
    ProteomesiUP000001991: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 332332Ferredoxin--NADP reductasePRO_0000364858Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi557436.Lreu_1657.

    Structurei

    3D structure databases

    ProteinModelPortaliA5VM22.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ferredoxin--NADP reductase type 2 family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0492.
    HOGENOMiHOG000072909.
    KOiK00384.
    OMAiTHYSKTV.
    OrthoDBiEOG661H9M.

    Family and domain databases

    HAMAPiMF_01685. FENR2.
    InterProiIPR013027. 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]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    PR00469. PNDRDTASEII.

    Sequencei

    Sequence statusi: Complete.

    A5VM22-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEKIYDVTI IGGGPAGMFA SFYCGLHELD AQLIESLPQL GGQVGALYPE    50
    KQVWDVAGMP GVTGHDLIAK LEEQMAVAPI DQFLGETVED VIKGDDGTFT 100
    IKSAKRVSRS RAVIIALGNG AFTPRKLALE GAAEIEGKQL SYFVNHKADY 150
    ADKRVAILGG GDSAIDIALM LEPVAKEVHL VHRRDQFRGL EHTVTQLKQS 200
    SVQLDTPFLP RALTVEDDET VTLDLKKMRS DDEAQLNVDK IVVNYGFTSN 250
    NAALNQWSLD LAAEHNLIKV DSMMETSTEG VYAIGDGVTY PGKVALIAAG 300
    FGEAPTAVTA LAKKLYPDKR MAMHSSSMGI TK 332
    Length:332
    Mass (Da):35,792
    Last modified:July 10, 2007 - v1
    Checksum:i6F0FFA8D88192A71
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000705 Genomic DNA. Translation: ABQ83896.1.
    RefSeqiYP_001272233.1. NC_009513.1.

    Genome annotation databases

    EnsemblBacteriaiABQ83896; ABQ83896; Lreu_1657.
    GeneIDi5189025.
    KEGGilre:Lreu_1657.
    PATRICi22256575. VBILacReu87937_1675.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000705 Genomic DNA. Translation: ABQ83896.1 .
    RefSeqi YP_001272233.1. NC_009513.1.

    3D structure databases

    ProteinModelPortali A5VM22.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 557436.Lreu_1657.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ83896 ; ABQ83896 ; Lreu_1657 .
    GeneIDi 5189025.
    KEGGi lre:Lreu_1657.
    PATRICi 22256575. VBILacReu87937_1675.

    Phylogenomic databases

    eggNOGi COG0492.
    HOGENOMi HOG000072909.
    KOi K00384.
    OMAi THYSKTV.
    OrthoDBi EOG661H9M.

    Enzyme and pathway databases

    BioCyci LREU557436:GC7Y-1740-MONOMER.

    Family and domain databases

    HAMAPi MF_01685. FENR2.
    InterProi IPR013027. 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 ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    PR00469. PNDRDTASEII.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 20016.

    Entry informationi

    Entry nameiFENR_LACRD
    AccessioniPrimary (citable) accession number: A5VM22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 3, 2009
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 60 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3