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    FAD/NAD(P)-binding oxidoreductase [ Arabidopsis thaliana (thale cress) ]

    Gene ID: 838079, updated on 18-Sep-2024

    Summary

    Official Full Name
    FAD/NAD(P)-binding oxidoreductase
    Primary source
    TAIR:AT1G15140
    Locus tag
    AT1G15140
    See related
    Araport:AT1G15140
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Arabidopsis thaliana (ecotype: Columbia)
    Lineage
    Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
    Also known as
    F9L1.8; F9L1_8
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    Try the new Transcript table

    Genomic context

    Location:
    chromosome: 1
    Exon count:
    5
    Sequence:
    Chromosome: 1; NC_003070.9 (5210181..5212349, complement)

    Chromosome 1 - NC_003070.9Genomic Context describing neighboring genes Neighboring gene Ubiquinol-cytochrome C reductase hinge protein Neighboring gene S-adenosyl-L-methionine-dependent methyltransferases superfamily protein Neighboring gene Endosomal targeting BRO1-like domain-containing protein Neighboring gene MATE efflux family protein Neighboring gene MATE efflux family protein

    Bibliography

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General protein information

    Preferred Names
    FAD/NAD(P)-binding oxidoreductase
    NP_563963.1
    • FAD/NAD(P)-binding oxidoreductase; FUNCTIONS IN: oxidoreductase activity, copper ion binding; INVOLVED IN: oxidation reduction; LOCATED IN: thylakoid, chloroplast, chloroplast stroma, chloroplast envelope; EXPRESSED IN: 23 plant structures; EXPRESSED DURING: 15 growth stages; CONTAINS InterPro DOMAIN/s: Oxidoreductase FAD/NAD(P)-binding (InterPro:IPR001433), Ferredoxin reductase-type FAD-binding domain (InterPro:IPR017927), Oxidoreductase, FAD-binding domain (InterPro:IPR008333), Riboflavin synthase-like beta-barrel (InterPro:IPR017938), Phenol hydroxylase reductase (InterPro:IPR001221); BEST Arabidopsis thaliana protein match is: ferredoxin-NADP(+)-oxidoreductase 2 (TAIR:AT1G20020.3); Has 6042 Blast hits to 6042 proteins in 1578 species: Archae - 81; Bacteria - 4817; Metazoa - 13; Fungi - 213; Plants - 309; Viruses - 0; Other Eukaryotes - 609 (source: NCBI BLink).
    NP_973832.1
    • FAD/NAD(P)-binding oxidoreductase; FUNCTIONS IN: oxidoreductase activity, copper ion binding; INVOLVED IN: oxidation reduction; LOCATED IN: thylakoid, chloroplast; EXPRESSED IN: 23 plant structures; EXPRESSED DURING: 15 growth stages; CONTAINS InterPro DOMAIN/s: Oxidoreductase FAD/NAD(P)-binding (InterPro:IPR001433), Ferredoxin reductase-type FAD-binding domain (InterPro:IPR017927), Oxidoreductase, FAD-binding domain (InterPro:IPR008333), Riboflavin synthase-like beta-barrel (InterPro:IPR017938), Phenol hydroxylase reductase (InterPro:IPR001221); BEST Arabidopsis thaliana protein match is: ferredoxin-NADP(+)-oxidoreductase 2 (TAIR:AT1G20020.3); Has 35333 Blast hits to 34131 proteins in 2444 species: Archae - 798; Bacteria - 22429; Metazoa - 974; Fungi - 991; Plants - 531; Viruses - 0; Other Eukaryotes - 9610 (source: NCBI BLink).
    NP_973833.1
    • FAD/NAD(P)-binding oxidoreductase; FUNCTIONS IN: oxidoreductase activity, copper ion binding; INVOLVED IN: oxidation reduction; LOCATED IN: thylakoid, chloroplast; EXPRESSED IN: 23 plant structures; EXPRESSED DURING: 15 growth stages; CONTAINS InterPro DOMAIN/s: Oxidoreductase FAD/NAD(P)-binding (InterPro:IPR001433), Ferredoxin reductase-type FAD-binding domain (InterPro:IPR017927), Oxidoreductase, FAD-binding domain (InterPro:IPR008333), Riboflavin synthase-like beta-barrel (InterPro:IPR017938), Phenol hydroxylase reductase (InterPro:IPR001221); BEST Arabidopsis thaliana protein match is: ferredoxin-NADP(+)-oxidoreductase 2 (TAIR:AT1G20020.3); Has 35333 Blast hits to 34131 proteins in 2444 species: Archae - 798; Bacteria - 22429; Metazoa - 974; Fungi - 991; Plants - 531; Viruses - 0; Other Eukaryotes - 9610 (source: NCBI BLink).

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_003070.9 Reference assembly

      Range
      5210181..5212349 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_101382.3NP_563963.1  FAD/NAD(P)-binding oxidoreductase [Arabidopsis thaliana]

      See identical proteins and their annotated locations for NP_563963.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      A0A178WAY6, Q9XI55
      Conserved Domains (1) summary
      cd00322
      Location:66289
      FNR_like; Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport ...
    2. NM_202104.2NP_973833.1  FAD/NAD(P)-binding oxidoreductase [Arabidopsis thaliana]

      See identical proteins and their annotated locations for NP_973833.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      F4HXZ3
      Conserved Domains (1) summary
      cl06868
      Location:92248
      FNR_like; Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport ...
    3. NM_202103.1NP_973832.1  FAD/NAD(P)-binding oxidoreductase [Arabidopsis thaliana]

      See identical proteins and their annotated locations for NP_973832.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      F4HXZ3
      Conserved Domains (1) summary
      cl06868
      Location:92248
      FNR_like; Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport ...