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Reviewed, UniProtKB/Swiss-Prot Q60365 (RIFK_METJA)

Last modified July 13, 2010. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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Names and originHide

Protein namesRecommended 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
OrganismMethanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]
Taxonomic identifier2190 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus
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Protein attributesHide

Sequence length136 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.
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General annotation (Comments)Hide

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. Ref.3

Catalytic activity

CTP + riboflavin = CDP + FMN. Ref.3

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. HAMAP MF_01285

Pathway

Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1. HAMAP MF_01285

Subunit structure

Monomer. Ref.3

Sequence similarities

Belongs to the archaeal riboflavin kinase family.

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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 136136Riboflavin kinase HAMAP MF_01285
PRO_0000106673

Regions

Nucleotide binding14 – 196CDP HAMAP MF_01285
Nucleotide binding112 – 1154CDP HAMAP MF_01285

Sites

Metal binding431Magnesium HAMAP MF_01285
Metal binding451Magnesium HAMAP MF_01285
Binding site991FMN HAMAP MF_01285
Binding site1001FMN HAMAP MF_01285
Binding site1071FMN HAMAP MF_01285

Secondary structure

1 ......................... 136
Helix Strand Turn

Details...

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SequencesHide

Sequence LengthMass (Da)Tools
Q60365-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 9F58C831BB21418C

FASTA13615,686
        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

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ReferencesHide

« Hide '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. expand/collapse author list , 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.
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ		L77117 Genomic DNA. Translation: AAB98036.1.
PIRH64306.
RefSeqNP_247020.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OYNX-ray1.85A2-136[»]
2P3MNMR-A1-136[»]
2VBSX-ray3.00A1-136[»]
2VBTX-ray2.70A1-136[»]
2VBUX-ray1.70A1-136[»]
2VBVX-ray2.40A/B1-136[»]
ModBaseSearch...

Genome annotation databases

GeneID1450895.
GenomeReviewsGene locus MJ0056 in contig L77117_GR.
KEGGmja:MJ0056.
NMPDRfig|243232.1.peg.57.
TIGRMJ0056.

Phylogenomic databases

HOGENOMHBG553349.
OMAPYEGTLN.
ProtClustDBPRK14132.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13864.

Family and domain databases

HAMAPMF_01285. Riboflavin_kinase.
[Tree]
InterProIPR002834. Riboflavin_kinase_arc.
[Graphical view]
PfamPF01982. CTP-dep_RFKase. 1 hit.
[Graphical view]
ProtoNetSearch...
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Entry informationHide

Entry nameRIFK_METJA
AccessionPrimary (citable) accession number: Q60365
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 13, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
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Relevant documentsHide

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents