Reviewed, UniProtKB/Swiss-Prot Q60365 (RIFK_METJA)

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:	MJ0056

Organism

Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]

Taxonomic identifier

2190 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN). Can also utilize UTP as the phosphate donor, although less efficiently, but cannot use neither ATP nor GTP.
Catalytic activity	CTP + riboflavin = CDP + FMN.
Cofactor	Binds 1 magnesium ion per subunit. This ion is coordinated by a threonine and an asparagine, and by the alpha- and beta-phosphates of CDP.
Pathway	Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin: step 1/1.
Subunit structure	Monomer.
Sequence similarities	Belongs to the archaeal riboflavin kinase family.

Ontologies

Keywords
Ligand	FMN Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	FMN biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	kinase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: HAMAP phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 136

136

Riboflavin kinase

Regions

Nucleotide binding

14 – 19

6

CDP

Nucleotide binding

112 – 115

4

CDP

Sites

Metal binding

43

1

Magnesium

Metal binding

45

1

Magnesium

Binding site

99

1

FMN

Binding site

100

1

FMN

Binding site

107

1

FMN

Secondary structure

1

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136

Helix Strand Turn

Details...

Beta strand

2 – 12

11

Helix

17 – 21

5

Helix

25 – 35

11

Beta strand

44 – 52

9

Helix

54 – 56

3

Beta strand

65 – 67

3

Beta strand

70 – 72

3

Beta strand

75 – 84

10

Beta strand

87 – 98

12

Beta strand

103 – 109

7

Helix

114 – 118

5

Beta strand

125 – 131

7

Sequences

	Sequence		Length	Mass (Da)
	Q60365-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 9F58C831BB21418C	FASTA	136	15,686
	10 20 30 40 50 60 MVKLMIIEGE VVSGLGEGRY FLSLPPYKEI FKKILGFEPY EGTLNLKLDR EFDINKFKYI 70 80 90 100 110 120 ETEDFEFNGK RFFGVKVLPI KILIGNKKID GAIVVPKKTY HSSEIIEIIA PMKLREQFNL 130 KDGDVIKILI KGDKDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"Crystal structure of hypothetical protein from Methanococcus jannaschii bound to CDP." New York structural genomics research consortium (NYSGRC) Submitted (MAR-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CDP.
[3]	"A CTP-dependent archaeal riboflavin kinase forms a bridge in the evolution of cradle-loop barrels." Ammelburg M., Hartmann M.D., Djuranovic S., Alva V., Koretke K.K., Martin J., Sauer G., Truffault V., Zeth K., Lupas A.N., Coles M. Structure 15:1577-1590(2007) [PubMed: 18073108] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH REACTION PRODUCTS AND MAGNESIUM, STRUCTURE BY NMR, FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION, SUBSTRATE SPECIFICITY, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L77117 Genomic DNA. Translation: AAB98036.1.

PIR

H64306.

RefSeq

NP_247020.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OYN	X-ray	1.85	A	1-136	[»]
2P3M	NMR	-	A	1-136	[»]
2VBS	X-ray	3.00	A	1-136	[»]
2VBT	X-ray	2.70	A	1-136	[»]
2VBU	X-ray	1.70	A	1-136	[»]
2VBV	X-ray	2.40	A/B	1-136	[»]

ModBase

Search...

Genome annotation databases

GeneID

1450895.

GenomeReviews

Gene locus MJ0056 in contig L77117_GR.

KEGG

mja:MJ0056.

NMPDR

fig|243232.1.peg.57.

TIGR

MJ0056.

Phylogenomic databases

HOGENOM

Q60365.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13864.
MJAN243232:MJ_0056-MON.

Family and domain databases

HAMAP

MF_01285.
[Tree]

InterPro

IPR002834. Riboflavin_kinase_arc.
[Graphical view]

Pfam

PF01982. DUF120. 1 hit.
[Graphical view]

ProDom

PD015839. DUF120. 1 hit.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

ProtoNet

Search...

Entry information

Entry name

RIFK_METJA

Accession

Primary (citable) accession number: Q60365

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	September 2, 2008
This is version 41 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)