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Q9L6L9 (FRE_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:STM3979
ORF Names:STMD1.10
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 233232NAD(P)H-flavin reductase
PRO_0000068147

Regions

Domain2 – 119118FAD-binding FR-type
Nucleotide binding111 – 1155Pyridine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9L6L9 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 200AE5691041B715

FASTA23326,351
        10         20         30         40         50         60 
MTTLSCKVTS VEAITDTVYR VRLVPDAAFS FRAGQYLMVV MDERDKRPFS MASTPDEKGF 

        70         80         90        100        110        120 
IELHIGASEL NLYAMAVMDR ILKDREIVVD IPHGDAWLRD DEERPLILIA GGTGFSYVRS 

       130        140        150        160        170        180 
ILLTALARNP ARDVTIYWGG REEKHLYDLS ELEALSVNHP NLRIEPVVEQ PEEGWRGRTG 

       190        200        210        220        230 
TVLTAVLQDY GTLAGHDIYI AGRFEMAKIA RDLFCHERNA REDRLFGDAF AFI 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"Reduction of Cob(III)alamin to Cob(II)alamin in Salmonella enterica serovar typhimurium LT2."
Fonseca M.V., Escalante-Semerena J.C.
J. Bacteriol. 182:4304-4309(2000) [PubMed: 10894741] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16, CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF233324 Genomic DNA. Translation: AAF33411.1.
AE006468 Genomic DNA. Translation: AAL22823.1.
RefSeqNP_462864.1. NC_003197.1.

3D structure databases

ProteinModelPortalQ9L6L9.
SMRQ9L6L9. Positions 2-233.
ModBaseSearch...

Proteomic databases

PRIDEQ9L6L9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1255505.
GenomeReviewsGene locus STM3979 in contig AE006468_GR.
KEGGstm:STM3979.
NMPDRfig|99287.1.peg.3838.
PATRIC32386825. VBISalEnt20916_4198.

Phylogenomic databases

HOGENOMHBG625960.
ProtClustDBPRK08051.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13237.
STYP99287:STM3979-MONOMER.

Family and domain databases

InterProIPR017927. 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]
KOK05368.
PfamPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00410. PHEHYDRXLASE.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRE_SALTY
AccessionPrimary (citable) accession number: Q9L6L9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families