Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Flavodoxin/ferredoxin--NADP reductase

Gene

fpr

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Transports electrons between flavodoxin or ferredoxin and NADPH (PubMed:8449868, PubMed:9839946, PubMed:12234497, PubMed:21306142). Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner (PubMed:12234497). Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and cobalamin-dependent methionine synthase (PubMed:7042345, PubMed:8267617).6 Publications

Caution

PubMed:2834327 authors incorrectly assigned the protein to be part of FPR, the C-terminal of GlpX.Curated

Catalytic activityi

2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.3 Publications
Reduced flavodoxin + NADP+ = oxidized flavodoxin + NADPH.2 Publications

Cofactori

FAD2 Publications

Kineticsi

kcat is 338.9 min(-1) with NADPH as the donor. kcat is 33 min(-1) with NADP as the donor (PubMed:11085917). kcat is 0.15 sec(-1) with ferredoxin as substrate. kcat is 0.0042 sec(-1) with flavodoxin 1 as substrate. kcat is 0.0039 sec(-1) with flavodoxin 2 as substrate (PubMed:12234497).2 Publications
  1. KM=3.85 µM for NADPH1 Publication
  2. KM=3.9 µM for NADPH1 Publication
  3. KM=2.04 mM for NADH1 Publication
  4. KM=12.0 µM for ferredoxin1 Publication
  5. KM=7.6 µM for flavodoxin 11 Publication
  6. KM=4.0 µM for flavodoxin 21 Publication
  7. KM=6.84 µM for flavodoxin1 Publication
  8. KM=17.6 µM for cytochrome c1 Publication
  9. KM=23.6 µM for potassium ferricyanide1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei17NADPCombined sources1 Publication1
    Binding sitei66FAD; via carbonyl oxygenCombined sources2 Publications1
    Binding sitei116FADCombined sources1 Publication1
    Binding sitei184NADPCombined sources1 Publication1
    Binding sitei220NADPCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi50 – 53FADCombined sources2 Publications4
    Nucleotide bindingi74 – 76FADCombined sources2 Publications3
    Nucleotide bindingi143 – 144NADPCombined sources1 Publication2
    Nucleotide bindingi173 – 174NADPCombined sources1 Publication2
    Nucleotide bindingi214 – 216NADPCombined sources1 Publication3
    Nucleotide bindingi247 – 248FADCombined sources1 Publication2

    GO - Molecular functioni

    • FAD binding Source: EcoCyc
    • ferredoxin-NADP+ reductase activity Source: EcoCyc
    • oxidoreductase activity Source: EcoliWiki

    GO - Biological processi

    • fructose catabolic process Source: EcoliWiki
    • iron-sulfur cluster assembly Source: EcoCyc
    • response to drug Source: EcoliWiki
    • response to superoxide Source: EcoCyc

    Keywordsi

    Molecular functionOxidoreductase
    LigandFAD, Flavoprotein, NADP, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:FLAVONADPREDUCT-MONOMER
    MetaCyc:FLAVONADPREDUCT-MONOMER
    BRENDAi1.18.1.2 2026

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Flavodoxin/ferredoxin--NADP reductaseCurated (EC:1.18.1.23 Publications, EC:1.19.1.12 Publications)
    Alternative name(s):
    Ferredoxin (flavodoxin):NADP(+) oxidoreductase1 Publication
    Ferredoxin--NADP reductase1 Publication
    Short name:
    FNR1 Publication
    Flavodoxin--NADP reductaseCurated
    Short name:
    FLDR1 Publication
    Methyl viologen resistance protein A1 Publication
    dA11 Publication
    Gene namesi
    Name:fpr1 Publication
    Synonyms:mvrA1 Publication
    Ordered Locus Names:b3924, JW3895
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11518 fpr

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    • cytosol Source: EcoCyc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Mutant is highly sensitive to methyl viologen.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi144R → A: Increases Km for NADPH. 2-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi174R → A: Increases Km for NADPH. 13-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi184R → A: Increases Km for NADPH. 15-fold decrease in catalytic efficiency. 1 Publication1

    Chemistry databases

    DrugBankiDB03147 Flavin adenine dinucleotide

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved2 Publications
    ChainiPRO_00001676432 – 248Flavodoxin/ferredoxin--NADP reductaseAdd BLAST247

    Proteomic databases

    EPDiP28861
    PaxDbiP28861
    PRIDEiP28861

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi4261115, 4 interactors
    IntActiP28861, 6 interactors
    STRINGi316385.ECDH10B_4113

    Structurei

    Secondary structure

    1248
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 14Combined sources11
    Beta strandi16 – 25Combined sources10
    Beta strandi36 – 41Combined sources6
    Beta strandi48 – 53Combined sources6
    Beta strandi61 – 68Combined sources8
    Helixi76 – 80Combined sources5
    Beta strandi87 – 93Combined sources7
    Helixi100 – 102Combined sources3
    Beta strandi107 – 114Combined sources8
    Helixi115 – 118Combined sources4
    Helixi119 – 127Combined sources9
    Beta strandi135 – 145Combined sources11
    Helixi146 – 148Combined sources3
    Helixi152 – 161Combined sources10
    Turni162 – 164Combined sources3
    Beta strandi165 – 175Combined sources11
    Beta strandi180 – 183Combined sources4
    Helixi185 – 190Combined sources6
    Helixi193 – 198Combined sources6
    Turni204 – 206Combined sources3
    Beta strandi207 – 213Combined sources7
    Helixi215 – 229Combined sources15
    Beta strandi236 – 238Combined sources3
    Beta strandi241 – 246Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1FDRX-ray1.70A1-248[»]
    2XNJX-ray1.90A/B2-247[»]
    ProteinModelPortaliP28861
    SMRiP28861
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28861

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini2 – 101FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST100

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105DP0 Bacteria
    COG1018 LUCA
    HOGENOMiHOG000265758
    InParanoidiP28861
    KOiK00528
    OMAiPFIAGQF
    PhylomeDBiP28861

    Family and domain databases

    CDDicd06195 FNR1, 1 hit
    InterProiView protein in InterPro
    IPR017927 Fd_Rdtase_FAD-bd
    IPR033892 FNR_bac
    IPR008333 OxRdtase_FAD-bd_dom
    IPR001433 OxRdtase_FAD/NAD-bd
    IPR017938 Riboflavin_synthase-like_b-brl
    PfamiView protein in Pfam
    PF00970 FAD_binding_6, 1 hit
    PF00175 NAD_binding_1, 1 hit
    SUPFAMiSSF63380 SSF63380, 1 hit
    PROSITEiView protein in PROSITE
    PS51384 FAD_FR, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P28861-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MADWVTGKVT KVQNWTDALF SLTVHAPVLP FTAGQFTKLG LEIDGERVQR
    60 70 80 90 100
    AYSYVNSPDN PDLEFYLVTV PDGKLSPRLA ALKPGDEVQV VSEAAGFFVL
    110 120 130 140 150
    DEVPHCETLW MLATGTAIGP YLSILQLGKD LDRFKNLVLV HAARYAADLS
    160 170 180 190 200
    YLPLMQELEK RYEGKLRIQT VVSRETAAGS LTGRIPALIE SGELESTIGL
    210 220 230 240
    PMNKETSHVM LCGNPQMVRD TQQLLKETRQ MTKHLRRRPG HMTAEHYW
    Length:248
    Mass (Da):27,751
    Last modified:January 23, 2007 - v4
    Checksum:iCBF46435A95709E4
    GO

    Sequence cautioni

    The sequence Z11767 differs from that shown. Reason: Frameshift at positions 94 and 127.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L04757 Genomic DNA Translation: AAA23805.1
    L19201 Genomic DNA Translation: AAB03056.1
    U00096 Genomic DNA Translation: AAC76906.1
    AP009048 Genomic DNA Translation: BAE77386.1
    Z11767 Genomic DNA No translation available.
    M19644 Genomic DNA Translation: AAA24189.1 Sequence problems.
    PIRiS40867
    RefSeqiNP_418359.1, NC_000913.3
    WP_000796332.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC76906; AAC76906; b3924
    BAE77386; BAE77386; BAE77386
    GeneIDi948414
    KEGGiecj:JW3895
    eco:b3924
    PATRICifig|1411691.4.peg.2781

    Similar proteinsi

    Entry informationi

    Entry nameiFENR_ECOLI
    AccessioniPrimary (citable) accession number: P28861
    Secondary accession number(s): P11007, Q2M8M0
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: January 23, 2007
    Last modified: March 28, 2018
    This is version 151 of the entry and version 4 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Cookie policy

    We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health