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 (By similarity).
CATALYTIC ACTIVITY: FMNH₂ + NAD(P)⁺ = FMN + NAD(P)H.
CATALYTIC ACTIVITY: 2 cob(II)alamin + NAD⁺ = 2 aquacob(III)alamin + NADH.
SUBUNIT: Monomer (By similarity).
SIMILARITY: Belongs to the fre/luxG FAD/NAD(P) flavoprotein oxidoreductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.

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

AE014075; AAN83224.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_756650.2; -.

3D structure databases

SMR

P0AEN2; 2-233.

ModBase

P0AEN2.

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

1035669; -.

GenomeReviews

AE014075_GR; c4791.

KEGG

ecc:c4791; -.

Phylogenomic databases

HOGENOM

P0AEN2; -.

Genome annotation databases

CMR

P0AEN2; c4791.

Other

ProtoNet

P0AEN2.

UniRef

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

Keywords

Complete proteome; 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 (By similarity).`
`CHAIN`	`2 233`	`232`	`NAD(P)H-flavin reductase.`	`PRO_0000068146`
`DOMAIN`	`2 99`	`98`	`FAD-binding FR-type.`
`NP_BIND`	`111 115`	`5`	`Pyridine (By similarity).`

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

P0AEN2 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