P0AEN3 (FRE_ECO57) Reviewed, UniProtKB/Swiss-Prot

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:	ubiB
Ordered Locus Names:	Z5365, ECs4772

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [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	Reduced riboflavin + NAD(P)+ = riboflavin + 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	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	1	1	Removed By similarity
	Chain	2 – 233	232	NAD(P)H-flavin reductase		PRO_0000068145
Regions
	Domain	2 – 99	98	FAD-binding FR-type
	Nucleotide binding	111 – 115	5	Pyridine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AEN3 [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

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG59038.1. BA000007 Genomic DNA. Translation: BAB38195.1.
PIR	B86072. D91225.
RefSeq	NP_290474.1. NC_002655.2. NP_312799.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0AEN3.
SMR	P0AEN3. Positions 2-233.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000025916; EBESCP00000024809; EBESCG00000024969. EBESCT00000060173; EBESCP00000058001; EBESCG00000059220.
GeneID	915131. 960316.
GenomeReviews	Gene locus Z5365 in contig AE005174_GR. Gene locus ECs4772 in contig BA000007_GR.
KEGG	ece:Z5365. ecs:ECs4772.
PATRIC	18359169. VBIEscCol44059_4739.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009405.
HOGENOM	HBG625960.
OMA	ARDLFCN.
ProtClustDB	PRK08051.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS4772-MONOMER.
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]
KO	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_ECO57

Accession

Primary (citable) accession number: P0AEN3
Secondary accession number(s): P23486, P76768

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program