Reviewed,
UniProtKB/Swiss-Prot P0AEN2 (FRE_ECOL6)
Last modified
June 16, 2009.
Version 30.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
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| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 217992 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 233 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ion transport Iron transport Transport |
| Ligand | FAD FMN Flavoprotein Iron NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | iron ion transport Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | FMN reductase activity Inferred from electronic annotation. Source: EC aquacobalamin reductase activityInferred from electronic annotation. Source: EC electron carrier activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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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. | |
| RefSeq | NP_756650.2. |
3D structure databases | |
| SMR | P0AEN2. Positions 2-233. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1035669. |
| GenomeReviews | Gene locus c4791 in contig AE014075_GR. |
| KEGG | ecc:c4791. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0AEN2. |
| OMA | P0AEN2. ETTLYWG. |
Enzyme and pathway databases | |
| BRENDA | 1.16.1.3. 292881. 1.5.1.29. 292881. |
Family and domain databases | |
| InterPro | IPR017927. Fd_Rdtase_FAD-bd. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. IPR001221. Phe_hydroxylase. [Graphical view] |
| Pfam | PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PRINTS | PR00410. PHEHYDRXLASE. |
| PROSITE | PS51384. FAD_FR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FRE_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: P0AEN2 Secondary accession number(s): P23486, P76768 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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