Reviewed, UniProtKB/Swiss-Prot Q2NHN9 (RIFK_METST)

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:	Msp_0177

Organism

Methanosphaera stadtmanae (strain DSM 3091) [Complete proteome] [HAMAP]

Taxonomic identifier

339860 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanosphaera

Protein attributes

Sequence length	131 AA.
Sequence status	Complete.
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. HAMAP MF_01285
Catalytic activity	CTP + riboflavin = CDP + FMN. HAMAP MF_01285
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01285
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 – 131	131	Riboflavin kinase HAMAP MF_01285		PRO_0000322076
Regions
	Nucleotide binding	11 – 16	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)
	Q2NHN9-1 [UniParc]. Last modified February 7, 2006. Version 1. Checksum: 3EBAFDE4DFB2EEDF	FASTA	131	14,886
	10 20 30 40 50 60 MLSFEGKVSS GLQKAGQFME KEVYKKQYLD KLGFIPYHGT LNIKLSNNIT LNLDNLHDKL 70 80 90 100 110 120 KRIHGNGSFG DVLFLEAYLS TIDEKITKKG AILFPVKTVY DTDTLEYVSS EKLRDTLNLK 130 DGDKVIIKIE K

References

[1]

"The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis." Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R., Gottschalk G., Thauer R.K. J. Bacteriol. 188:642-658(2006) [PubMed: 16385054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000102 Genomic DNA. Translation: ABC56594.1.
RefSeq	YP_447237.1.
3D structure databases
SMR	Q2NHN9. Positions 1-130.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2NHN9.
Genome annotation databases
GeneID	3856051.
GenomeReviews	Gene locus Msp_0177 in contig CP000102_GR.
KEGG	mst:Msp_0177.
NMPDR	fig|339860.6.peg.174.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG10832.
HOGENOM	HBG553349.
Enzyme and pathway databases
BioCyc	MSTA339860:MSP_0177-MONOMER.
Family and domain databases
HAMAP	MF_01285. Riboflavin_kinase. [Tree]
InterPro	IPR002834. Riboflavin_kinase_arc. [Graphical view]
Pfam	PF01982. CTP-dep_RFKase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIFK_METST

Accession

Primary (citable) accession number: Q2NHN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	February 7, 2006
Last modified:	January 19, 2010
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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