Reviewed, UniProtKB/Swiss-Prot Q9YA27 (RIFK_AERPE)

Names and origin

Protein names

Recommended name:
    Riboflavin kinase
      Short name=RFK
    EC=2.7.1.161
Alternative name(s):
    CTP:riboflavin 5'-phosphotransferase
    CTP-dependent riboflavin kinase
    Flavokinase

Gene names

Name:	rfk
Ordered Locus Names:	APE_2112.1

Organism

Aeropyrum pernix [Complete proteome] [HAMAP]

Taxonomic identifier

56636 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length	132 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) By similarity.
Catalytic activity	CTP + riboflavin = CDP + FMN. HAMAP MF_01285
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1. HAMAP MF_01285
Sequence similarities	Belongs to the archaeal riboflavin kinase family.

Ontologies

Keywords
Ligand	FMN Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	FMN biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: HAMAP riboflavin kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 132	132	Riboflavin kinase HAMAP MF_01285		PRO_0000322065
Regions
	Nucleotide binding	13 – 18	6	CDP By similarity
	Nucleotide binding	111 – 114	4	CDP By similarity
Sites
	Metal binding	40	1	Magnesium By similarity
	Metal binding	42	1	Magnesium By similarity
	Binding site	98	1	FMN By similarity
	Binding site	106	1	FMN By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9YA27-1 [UniParc]. Last modified November 14, 2006. Version 2. Checksum: 992AB143E6CF1D05	FASTA	132	14,456
	10 20 30 40 50 60 MDCGVFEGTV FSGLGHGSFY VSIYARNLRR ALGYTPYPGT LNLRVGDAAE RLAGCIERAR 70 80 90 100 110 120 GVRIEPPPIP GERLASVLAF PVEIEGGVRG HIVRPEITVY KGDVVEIVAD VYLRDVLKIS 130 DGDKVRFRLL DP

References

[1]

"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H. DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000002 Genomic DNA. Translation: BAA81123.2.
PIR	C72517.
RefSeq	NP_148391.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1445199.
GenomeReviews	Gene locus APE_2112.1 in contig BA000002_GR.
KEGG	ape:APE_2112.1.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9YA27.
OMA	KTTHEEN.
Family and domain databases
HAMAP	MF_01285. [Tree]
InterPro	IPR002834. Riboflavin_kinase_arc. [Graphical view]
Pfam	PF01982. CTP-dep_RFKase. 1 hit. [Graphical view]
ProDom	PD015839. DUF120. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

RIFK_AERPE

Accession

Primary (citable) accession number: Q9YA27

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	November 14, 2006
Last modified:	November 3, 2009
This is version 41 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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