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Q8U262 (RIFK_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Riboflavin kinase

Short name=RFK
EC=2.7.1.161
Alternative name(s):
CTP-dependent riboflavin kinase
CTP:riboflavin 5'-phosphotransferase
Flavokinase
Gene names
Name:ribK
Ordered Locus Names:PF0988
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Riboflavin kinase HAMAP MF_01285
PRO_0000322102

Regions

Nucleotide binding97 – 1026CDP By similarity
Nucleotide binding193 – 1964CDP By similarity
Region1 – 8787H-T-H motif-like HAMAP MF_01285
Region88 – 212125Riboflavin kinase HAMAP MF_01285

Sites

Metal binding1241Magnesium By similarity
Metal binding1261Magnesium By similarity
Binding site1801FMN By similarity
Binding site1881FMN By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8U262 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: F2AB341CB6E2070A

FASTA21223,813
        10         20         30         40         50         60 
MKKSNLDLLI LLAKAGGIEK EILTTSRELS KMLNVSPQTI VRWLEDLEKD GLIKKSESRK 

        70         80         90        100        110        120 
GTLVTITEEG VKFLEKLHEE LSDALYRGII IGEVVSGIGE GAYYVRQYAP LIREYLGFDP 

       130        140        150        160        170        180 
YPGTLNVRVI FPKTIFDALC NVRPIIIPGF TKEGRTFGDV RAYRVKIDNI EGAIVIPSRT 

       190        200        210 
IHPPKIAEII APVNLRKTLN LKDGDRIRIK TL 

« Hide

References

[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009950 Genomic DNA. Translation: AAL81112.1.
RefSeqNP_578717.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ8U262.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000006014; EBPYRP00000005875; EBPYRG00000006013.
GeneID1468853.
GenomeReviewsGene locus PF0988 in contig AE009950_GR.
KEGGpfu:PF0988.
NMPDRfig|186497.1.peg.1024.

Phylogenomic databases

GeneTreeEBGT00050000023005.
HOGENOMHBG553349.
OMAGRHYISL.
ProtClustDBCLSK253495.

Family and domain databases

HAMAPMF_01285. Riboflavin_kinase. Fused.
[Tree]
InterProIPR023470. Riboflavin_kinase_archaeal.
IPR023602. Riboflavin_kinase_CTP-dep.
IPR023465. Riboflavin_kinase_domain.
IPR000835. Tscrpt_reg_HTH_MarR-typ.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:2.40.30.30. Riboflavin_kinase. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KOK07732.
PfamPF01982. CTP-dep_RFKase. 1 hit.
PF01047. MarR. 1 hit.
[Graphical view]
PROSITEPS50995. HTH_MARR_2. 1 hit. Uncertain.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIFK_PYRFU
AccessionPrimary (citable) accession number: Q8U262
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 1, 2002
Last modified: November 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families