Reviewed, UniProtKB/Swiss-Prot P0AEN1 (FRE_ECOLI)

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

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

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

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 reduces the complexed Fe3+ iron of siderophores to Fe2+, thus releasing it from the chelator.
Catalytic activity	FMNH2 + NAD(P)+ = FMN + 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
Gene Ontology (GO)
Biological process	iron ion transport Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN reductase activity Inferred from electronic annotation. Source: EC aquacobalamin reductase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 233

232

NAD(P)H-flavin reductase

PRO_0000068144

Regions

Domain

2 – 99

98

FAD-binding FR-type

Nucleotide binding

111 – 115

5

Pyridine By similarity

Secondary structure

1

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233

Helix Strand Turn

Details...

Beta strand

3 – 17

15

Beta strand

19 – 27

9

Beta strand

36 – 44

9

Beta strand

46 – 50

5

Beta strand

61 – 65

5

Helix

75 – 84

10

Beta strand

85 – 93

9

Beta strand

102 – 104

3

Beta strand

106 – 111

6

Helix

115 – 128

14

Beta strand

134 – 142

9

Helix

143 – 145

3

Helix

149 – 158

10

Beta strand

162 – 170

9

Beta strand

177 – 180

4

Helix

182 – 189

8

Beta strand

197 – 202

6

Helix

204 – 217

14

Helix

222 – 224

3

Helix

229 – 232

4

Sequences

	Sequence		Length	Mass (Da)
	P0AEN1-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 0E64DE5A8FA0F12D	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

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

AP_003958.1.
NP_418286.1.

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0AEN1.

Genome annotation databases

GeneID

948325.

GenomeReviews

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

KEGG

ecj:JW3820.
eco:b3844.

Organism-specific databases

EchoBASE

EB0330.

EcoGene

EG10334. fre.

CMR

Search...

Phylogenomic databases

eggNOG

COG0543.

HOGENOM

HBG625960.

OMA

DAMYYES.

Enzyme and pathway databases

BioCyc

EcoCyc:FMNREDUCT-MONOMER.
ECOL168927:B3844-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]

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_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 19, 2010
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)