[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21. PubMed=2050627 [NCBI, ExPASy, EBI, Israel, Japan] Spyrou G., Haggaard-Ljungquist E., Krook M., Joernvall H., Nilsson E., Reichard P.; "Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme."; J. Bacteriol. 173:3673-3679(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; Dirusso C.C., Shea O.; "FadI: identification, characterization, and nucleotide sequence of a gene required for full activation of structural genes of the AD regulon in Escherichia coli."; Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; Saviranta P.J.; Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; PubMed=1379743 [NCBI, ExPASy, EBI, Israel, Japan] Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.; "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."; Science 257:771-778(1992).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[7]	CHARACTERIZATION. STRAIN=K12; DOI=10.1016/0014-5793(92)80452-M; PubMed=1601132 [NCBI, ExPASy, EBI, Israel, Japan] Andrews S.C., Shipley D., Keen J.N., Findlay J.B.C., Harrison P.M., Guest J.R.; "The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductases."; FEBS Lett. 302:247-252(1992).
[8]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). DOI=10.1021/bi982849m; PubMed=10353815 [NCBI, ExPASy, EBI, Israel, Japan] Ingelman M., Ramaswamy S., Niviere V., Fontecave M., Eklund H.; "Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli."; Biochemistry 38:7040-7049(1999).

Comments

FUNCTION: Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides. Seems to reduces the complexed Fe(3+) iron of siderophores to Fe(2+), thus releasing it from the chelator.
CATALYTIC ACTIVITY: FMNH₂ + NAD(P)⁺ = FMN + NAD(P)H.
CATALYTIC ACTIVITY: 2 cob(II)alamin + NAD⁺ = 2 aquacob(III)alamin + NADH.
SUBUNIT: Monomer.
SIMILARITY: Belongs to the fre/luxG FAD/NAD(P) flavoprotein oxidoreductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
CAUTION: Was originally (PubMed:1379743) assigned to be ubiB.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M61182; AAA23806.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M85227; AAA23753.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M74448; AAA91058.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M87049; AAA67641.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76847.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77459.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A39434; A39434.

RefSeq

AP_003958.1; -.
NP_418286.1; -.

3D structure databases

PDB

1QFJ; X-ray; 2.20 A; A/B/C/D=1-233.

[ExPASy / RCSB / EBI]

PDBsum

1QFJ; -.

ModBase

P0AEN1.

Enzyme and pathway databases

BioCyc

EcoCyc:FMNREDUCT-MON; -.
MetaCyc:FMNREDUCT-MON; -.

Organism-specific databases

EchoBASE

EB0330; -.

EcoGene

EG10334; fre.

Ontologies

GO:0047138;	Molecular function: aquacobalamin reductase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0008752;	Molecular function: FMN reductase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006826;	Biological process: iron ion transport (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR001221; Phe_hydroxylase.
Graphical view of domain structure.

Pfam

PF00970; FAD_binding_6; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00410; PHEHYDRXLASE.

PROSITE

PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

948325; -.

GenomeReviews

AP009048_GR; JW3820.
U00096_GR; b3844.

KEGG

ecj:JW3820; -.
eco:b3844; -.

Phylogenomic databases

HOGENOM

P0AEN1; -.

Genome annotation databases

CMR

P0AEN1; b3844.

Other

ProtoNet

P0AEN1.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; FMN; Ion transport; Iron; Iron transport; NAD; NADP; Oxidoreductase; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 233`	`232`	`NAD(P)H-flavin reductase.`	`PRO_0000068144`
`DOMAIN`	`2 99`	`98`	`FAD-binding FR-type.`
`NP_BIND`	`111 115`	`5`	`Pyridine (By similarity).`
`STRAND`	`3 17`	`15`
`STRAND`	`19 27`	`9`
`STRAND`	`36 44`	`9`
`STRAND`	`46 50`	`5`
`STRAND`	`61 65`	`5`
`HELIX`	`75 84`	`10`
`STRAND`	`85 93`	`9`
`STRAND`	`102 104`	`3`
`STRAND`	`106 111`	`6`
`HELIX`	`115 128`	`14`
`STRAND`	`134 142`	`9`
`HELIX`	`143 145`	`3`
`HELIX`	`149 158`	`10`
`STRAND`	`162 170`	`9`
`STRAND`	`177 180`	`4`
`HELIX`	`182 189`	`8`
`STRAND`	`197 202`	`6`
`HELIX`	`204 217`	`14`
`HELIX`	`222 224`	`3`
`HELIX`	`229 232`	`4`

Sequence information

Length: 233 AA [This is the length of the unprocessed precursor]

Molecular weight: 26242 Da [This is the MW of the unprocessed precursor]

CRC64: 0E64DE5A8FA0F12D [This is a checksum on the sequence]

        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

P0AEN1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools