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Reviewed, UniProtKB/Swiss-Prot P0AEN2 (FRE_ECOL6)

Last modified June 16, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NAD(P)H-flavin reductase
    EC=1.5.1.29
    EC=1.16.1.3
Alternative name(s):
    FMN reductase
    NAD(P)H:flavin oxidoreductase
    Aquacobalamin reductase
    Ferrisiderophore reductase C
Gene names
Name: fre
Synonyms: ubiB
Ordered Locus Names: c4791
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

FMNH2 + NAD(P)+ = FMN + NAD(P)H.

2 cob(II)alamin + NAD+ = 2 aquacob(III)alamin + NADH.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the fre/luxG FAD/NAD(P) flavoprotein oxidoreductase family.

Contains 1 FAD-binding FR-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 233232NAD(P)H-flavin reductase
PRO_0000068146

Regions

Domain2 – 9998FAD-binding FR-type
Nucleotide binding111 – 1155Pyridine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AEN2-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0E64DE5A8FA0F12D

FASTA23326,242
        10         20         30         40         50         60 
MTTLSCKVTS VEAITDTVYR VRIVPDAAFS FRAGQYLMVV MDERDKRPFS MASTPDEKGF 

        70         80         90        100        110        120 
IELHIGASEI NLYAKAVMDR ILKDHQIVVD IPHGEAWLRD DEERPMILIA GGTGFSYARS 

       130        140        150        160        170        180 
ILLTALARNP NRDITIYWGG REEQHLYDLC ELEALSLKHP GLQVVPVVEQ PEAGWRGRTG 

       190        200        210        220        230 
TVLTAVLQDH GTLAEHDIYI AGRFEMAKIA RDLFCSERNA REDRLFGDAF AFI 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

AE014075 Genomic DNA. Translation: AAN83224.1. Different initiation.
RefSeqNP_756650.2.

3D structure databases

SMRP0AEN2. Positions 2-233.
ModBaseSearch...

Genome annotation databases

GeneID1035669.
GenomeReviewsGene locus c4791 in contig AE014075_GR.
KEGGecc:c4791.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP0AEN2.
OMAP0AEN2. ETTLYWG.

Enzyme and pathway databases

BRENDA1.16.1.3. 292881.
1.5.1.29. 292881.

Family and domain databases

InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR008333. OxRdtase_FAD-bd.
IPR001433. OxRdtase_FAD/NAD_bd.
IPR001221. Phe_hydroxylase.
[Graphical view]
PfamPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00410. PHEHYDRXLASE.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRE_ECOL6
AccessionPrimary (citable) accession number: P0AEN2
Secondary accession number(s): P23486, P76768
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 30 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents