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

Ferredoxin--NADP reductase

Gene

fpr

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transports electrons between flavodoxin or ferredoxin and NADPH. Involved in the reductive activation of cobalamin-independent methionine synthase, pyruvate formate lyase and anaerobic ribonucleotide reductase. Also protects against superoxide radicals due to methyl viologen in the presence of oxygen.

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531NADPBy similarity
Binding sitei66 – 661FAD; via carbonyl oxygen1 Publication
Binding sitei116 – 1161FAD1 Publication
Binding sitei116 – 1161NADP; via amide nitrogenBy similarity
Binding sitei245 – 2451NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi50 – 534FAD1 Publication
Nucleotide bindingi74 – 763FAD1 Publication
Nucleotide bindingi143 – 1442NADPBy similarity
Nucleotide bindingi173 – 1742NADPBy similarity
Nucleotide bindingi213 – 2142NADPBy similarity
Nucleotide bindingi247 – 2482FAD1 Publication

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
  • response to drug Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciEcoCyc:FLAVONADPREDUCT-MONOMER.
ECOL316407:JW3895-MONOMER.
MetaCyc:FLAVONADPREDUCT-MONOMER.
BRENDAi1.18.1.2. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin--NADP reductase (EC:1.18.1.2)
Short name:
FNR
Alternative name(s):
DA1
Flavodoxin reductase
Short name:
FLDR
Short name:
FLXR
Methyl viologen resistance protein A
Gene namesi
Name:fpr
Synonyms:mvrA
Ordered Locus Names:b3924, JW3895
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11518. fpr.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 248247Ferredoxin--NADP reductasePRO_0000167643Add
BLAST

Proteomic databases

EPDiP28861.
PaxDbiP28861.
PRIDEiP28861.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4261115. 2 interactions.
IntActiP28861. 6 interactions.
STRINGi511145.b3924.

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1411Combined sources
Beta strandi16 – 2510Combined sources
Beta strandi36 – 416Combined sources
Beta strandi48 – 536Combined sources
Beta strandi61 – 688Combined sources
Helixi76 – 805Combined sources
Beta strandi87 – 937Combined sources
Helixi100 – 1023Combined sources
Beta strandi107 – 1148Combined sources
Helixi115 – 1184Combined sources
Helixi119 – 1279Combined sources
Beta strandi135 – 14511Combined sources
Helixi146 – 1483Combined sources
Helixi152 – 16110Combined sources
Turni162 – 1643Combined sources
Beta strandi165 – 17511Combined sources
Beta strandi180 – 1834Combined sources
Helixi185 – 1906Combined sources
Helixi193 – 1986Combined sources
Turni204 – 2063Combined sources
Beta strandi207 – 2137Combined sources
Helixi215 – 22915Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi241 – 2466Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP28861.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 101100FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105DP0. Bacteria.
COG1018. LUCA.
HOGENOMiHOG000265758.
InParanoidiP28861.
KOiK00528.
OMAiPFIAGQF.
PhylomeDBiP28861.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

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.
PATRICi32123361. VBIEscCol129921_4041.

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

BioGridi4261115. 2 interactions.
IntActiP28861. 6 interactions.
STRINGi511145.b3924.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

EPDiP28861.
PaxDbiP28861.
PRIDEiP28861.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76906; AAC76906; b3924.
BAE77386; BAE77386; BAE77386.
GeneIDi948414.
KEGGiecj:JW3895.
eco:b3924.
PATRICi32123361. VBIEscCol129921_4041.

Organism-specific databases

EchoBASEiEB1480.
EcoGeneiEG11518. fpr.

Phylogenomic databases

eggNOGiENOG4105DP0. Bacteria.
COG1018. LUCA.
HOGENOMiHOG000265758.
InParanoidiP28861.
KOiK00528.
OMAiPFIAGQF.
PhylomeDBiP28861.

Enzyme and pathway databases

BioCyciEcoCyc:FLAVONADPREDUCT-MONOMER.
ECOL316407:JW3895-MONOMER.
MetaCyc:FLAVONADPREDUCT-MONOMER.
BRENDAi1.18.1.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP28861.
PROiP28861.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFENR_ECOLI
AccessioniPrimary (citable) accession number: P28861
Secondary accession number(s): P11007, Q2M8M0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.