Reviewed, UniProtKB/Swiss-Prot Q9L6L9 (FRE_SALTY)

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:	ubiB
Ordered Locus Names:	STM3979
ORF Names:	STMD1.10

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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 By similarity.
Catalytic activity	FMNH2 + NAD(P)+ = FMN + 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 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 By similarity
	Chain	2 – 233	232	NAD(P)H-flavin reductase		PRO_0000068147
Regions
	Domain	2 – 119	118	FAD-binding FR-type
	Nucleotide binding	111 – 115	5	Pyridine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9L6L9-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 200AE5691041B715	FASTA	233	26,351
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF233324 Genomic DNA. Translation: AAF33411.1. AE006468 Genomic DNA. Translation: AAL22823.1.
RefSeq	NP_462864.1.
3D structure databases
SMR	Q9L6L9. Positions 2-233.
ModBase	Search...
Proteomic databases
PRIDE	Q9L6L9.
Genome annotation databases
GeneID	1255505.
GenomeReviews	Gene locus STM3979 in contig AE006468_GR.
KEGG	stm:STM3979.
NMPDR	fig|99287.1.peg.3838.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG625960.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13237. STYP99287:STM3979-MONOMER.
BRENDA	1.16.1.3. 2. 1.5.1.29. 2.
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_SALTY

Accession

Primary (citable) accession number: Q9L6L9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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