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Protein

NAD(P)H-flavin reductase

Gene

fre

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

Functioni

Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides. Seems to reduce the complexed Fe3+ iron of siderophores to Fe2+, thus releasing it from the chelator.

Catalytic activityi

Reduced riboflavin + NAD(P)+ = riboflavin + NAD(P)H.
2 cob(II)alamin + NAD+ + 2 H2O = 2 aquacob(III)alamin + NADH.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi111 – 115PyridineBy similarity5

GO - Molecular functioni

  • aquacobalamin reductase activity Source: UniProtKB-EC
  • enzyme activator activity Source: EcoCyc
  • FAD binding Source: GO_Central
  • FMN reductase (NADPH) activity Source: Reactome
  • riboflavin reductase (NADH) activity Source: EcoCyc
  • riboflavin reductase (NADPH) activity Source: EcoCyc

GO - Biological processi

  • ion transport Source: UniProtKB-KW
  • iron ion homeostasis Source: UniProtKB-KW
  • protein repair Source: EcoCyc
  • response to oxidative stress Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, FMN, Iron, NAD, NADP

Enzyme and pathway databases

BioCyciEcoCyc:FMNREDUCT-MONOMER.
ECOL316407:JW3820-MONOMER.
MetaCyc:FMNREDUCT-MONOMER.
BRENDAi1.5.1.41. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P)H-flavin reductase (EC:1.16.1.3, EC:1.5.1.41)
Alternative name(s):
Aquacobalamin reductase
FMN reductase
Ferrisiderophore reductase C
NAD(P)H:flavin oxidoreductase
Riboflavin reductase [NAD(P)H]
Gene namesi
Name:fre
Synonyms:fadI, flrD, fsrC, ubiB
Ordered Locus Names:b3844, JW3820
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10334. fre.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000681442 – 233NAD(P)H-flavin reductaseAdd BLAST232

Proteomic databases

EPDiP0AEN1.
PaxDbiP0AEN1.
PRIDEiP0AEN1.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4262003. 8 interactors.
IntActiP0AEN1. 13 interactors.
STRINGi511145.b3844.

Structurei

Secondary structure

1233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 17Combined sources15
Beta strandi19 – 27Combined sources9
Beta strandi36 – 44Combined sources9
Beta strandi46 – 50Combined sources5
Beta strandi61 – 65Combined sources5
Helixi75 – 84Combined sources10
Beta strandi85 – 93Combined sources9
Beta strandi102 – 104Combined sources3
Beta strandi106 – 111Combined sources6
Helixi115 – 128Combined sources14
Beta strandi134 – 142Combined sources9
Helixi143 – 145Combined sources3
Helixi149 – 158Combined sources10
Beta strandi162 – 170Combined sources9
Beta strandi177 – 180Combined sources4
Helixi182 – 189Combined sources8
Beta strandi197 – 202Combined sources6
Helixi204 – 217Combined sources14
Helixi222 – 224Combined sources3
Helixi229 – 232Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QFJX-ray2.20A/B/C/D2-233[»]
ProteinModelPortaliP0AEN1.
SMRiP0AEN1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEN1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 99FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST98

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108EX3. Bacteria.
COG0543. LUCA.
HOGENOMiHOG000269618.
InParanoidiP0AEN1.
KOiK05368.
OMAiAREWHDA.
PhylomeDBiP0AEN1.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00410. PHEHYDRXLASE.
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.

P0AEN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTLSCKVTS VEAITDTVYR VRIVPDAAFS FRAGQYLMVV MDERDKRPFS
60 70 80 90 100
MASTPDEKGF IELHIGASEI NLYAKAVMDR ILKDHQIVVD IPHGEAWLRD
110 120 130 140 150
DEERPMILIA GGTGFSYARS ILLTALARNP NRDITIYWGG REEQHLYDLC
160 170 180 190 200
ELEALSLKHP GLQVVPVVEQ PEAGWRGRTG TVLTAVLQDH GTLAEHDIYI
210 220 230
AGRFEMAKIA RDLFCSERNA REDRLFGDAF AFI
Length:233
Mass (Da):26,242
Last modified:January 23, 2007 - v2
Checksum:i0E64DE5A8FA0F12D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61182 Genomic DNA. Translation: AAA23806.1.
M85227 Genomic DNA. Translation: AAA23753.1.
M74448 Genomic DNA. Translation: AAA91058.1.
M87049 Genomic DNA. Translation: AAA67641.1.
U00096 Genomic DNA. Translation: AAC76847.1.
AP009048 Genomic DNA. Translation: BAE77459.1.
PIRiA39434.
RefSeqiNP_418286.1. NC_000913.3.
WP_000209826.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76847; AAC76847; b3844.
BAE77459; BAE77459; BAE77459.
GeneIDi948325.
KEGGiecj:JW3820.
eco:b3844.
PATRICi32123185. VBIEscCol129921_3958.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61182 Genomic DNA. Translation: AAA23806.1.
M85227 Genomic DNA. Translation: AAA23753.1.
M74448 Genomic DNA. Translation: AAA91058.1.
M87049 Genomic DNA. Translation: AAA67641.1.
U00096 Genomic DNA. Translation: AAC76847.1.
AP009048 Genomic DNA. Translation: BAE77459.1.
PIRiA39434.
RefSeqiNP_418286.1. NC_000913.3.
WP_000209826.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QFJX-ray2.20A/B/C/D2-233[»]
ProteinModelPortaliP0AEN1.
SMRiP0AEN1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262003. 8 interactors.
IntActiP0AEN1. 13 interactors.
STRINGi511145.b3844.

Proteomic databases

EPDiP0AEN1.
PaxDbiP0AEN1.
PRIDEiP0AEN1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76847; AAC76847; b3844.
BAE77459; BAE77459; BAE77459.
GeneIDi948325.
KEGGiecj:JW3820.
eco:b3844.
PATRICi32123185. VBIEscCol129921_3958.

Organism-specific databases

EchoBASEiEB0330.
EcoGeneiEG10334. fre.

Phylogenomic databases

eggNOGiENOG4108EX3. Bacteria.
COG0543. LUCA.
HOGENOMiHOG000269618.
InParanoidiP0AEN1.
KOiK05368.
OMAiAREWHDA.
PhylomeDBiP0AEN1.

Enzyme and pathway databases

BioCyciEcoCyc:FMNREDUCT-MONOMER.
ECOL316407:JW3820-MONOMER.
MetaCyc:FMNREDUCT-MONOMER.
BRENDAi1.5.1.41. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AEN1.
PROiP0AEN1.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00410. PHEHYDRXLASE.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFRE_ECOLI
AccessioniPrimary (citable) accession number: P0AEN1
Secondary accession number(s): P23486, P76768, Q2M8E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally assigned to be ubiB.1 Publication

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.