NAD(P)H-flavin reductase - Escherichia coli (strain K12)

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P0AEN1 (FRE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	fre
Synonyms:	fadI, flrD, fsrC, ubiB
Ordered Locus Names:	b3844, JW3820

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [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	Evidence at protein level

General annotation (Comments)

Function	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 activity	Reduced riboflavin + NAD(P)⁺ = riboflavin + NAD(P)H. 2 cob(II)alamin + NAD⁺ = 2 aquacob(III)alamin + NADH.
Subunit structure	Monomer.
Sequence similarities	Belongs to the fre/luxG FAD/NAD(P) flavoprotein oxidoreductase family. Contains 1 FAD-binding FR-type domain.
Caution	Was originally (Ref.4) assigned to be ubiB.

Ontologies

Keywords
Biological process	Ion transport Iron transport Transport
Ligand	FAD FMN Flavoprotein Iron NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ion transport Inferred from electronic annotation. Source: UniProtKB-KW iron ion homeostasis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aquacobalamin reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1

Chain

2 – 233

232

NAD(P)H-flavin reductase

PRO_0000068144

Regions

Domain

2 – 99

FAD-binding FR-type

Nucleotide binding

111 – 115

Pyridine By similarity

Secondary structure

233

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AEN1 [UniParc].

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

233

26,242

        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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme." Spyrou G., Haggaard-Ljungquist E., Krook M., Joernvall H., Nilsson E., Reichard P. J. Bacteriol. 173:3673-3679(1991) [PubMed: 2050627] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21.
[2]	"FadI: identification, characterization, and nucleotide sequence of a gene required for full activation of structural genes of the AD regulon in Escherichia coli." Dirusso C.C., Shea O. Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	Saviranta P.J. Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[4]	"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R. Science 257:771-778(1992) [PubMed: 1379743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductases." Andrews S.C., Shipley D., Keen J.N., Findlay J.B.C., Harrison P.M., Guest J.R. FEBS Lett. 302:247-252(1992) [PubMed: 1601132] [Abstract] Cited for: CHARACTERIZATION. Strain: K12.
[8]	"Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli." Ingelman M., Ramaswamy S., Niviere V., Fontecave M., Eklund H. Biochemistry 38:7040-7049(1999) [PubMed: 10353815] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A39434.

RefSeq

NP_418286.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QFJ	X-ray	2.20	A/B/C/D	2-233	[»]

ProteinModelPortal

P0AEN1.

SMR

P0AEN1. Positions 2-233.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AEN1. 13 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000002824; EBESCP00000002824; EBESCG00000002302.
EBESCT00000017302; EBESCP00000016593; EBESCG00000016359.

GeneID

948325.

GenomeReviews

Gene locus JW3820 in contig AP009048_GR.
Gene locus b3844 in contig U00096_GR.

KEGG

ecj:JW3820.
eco:b3844.

PATRIC

32123185. VBIEscCol129921_3958.

Organism-specific databases

EchoBASE

EB0330.

EcoGene

EG10334. fre.

Phylogenomic databases

eggNOG

COG0543.

GeneTree

EBGT00050000009405.

HOGENOM

HBG625960.

OMA

ARDLFCN.

PhylomeDB

P0AEN1.

ProtClustDB

PRK08051.

Enzyme and pathway databases

BioCyc

EcoCyc:FMNREDUCT-MONOMER.
MetaCyc:FMNREDUCT-MONOMER.

Gene expression databases

Genevestigator

P0AEN1.

Family and domain databases

InterPro

IPR017927. 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]

K05368.

Pfam

PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]

PRINTS

PR00410. PHEHYDRXLASE.

SUPFAM

SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.

PROSITE

PS51384. FAD_FR. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FRE_ECOLI

Accession

Primary (citable) accession number: P0AEN1
Secondary accession number(s): P23486, P76768, Q2M8E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents