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A3MV29 (RIFK_PYRCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:Pcal_1071
OrganismPyrobaculum calidifontis (strain JCM 11548 / VA1) [Complete proteome] [HAMAP]
Taxonomic identifier410359 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

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_0000322101

Regions

Nucleotide binding93 – 986CDP By similarity
Nucleotide binding192 – 1954CDP By similarity
Region1 – 8383Unknown HAMAP MF_01285
Region84 – 212129Riboflavin kinase HAMAP MF_01285

Sites

Metal binding1221Magnesium By similarity
Metal binding1241Magnesium By similarity
Binding site1791FMN By similarity
Binding site1871FMN By similarity

Sequences

Sequence LengthMass (Da)Tools
A3MV29 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 55FB8E799B8F28F1

FASTA21223,505
        10         20         30         40         50         60 
MTELYCERKT LADLIAFASV EGLPVGEAAK RLCMSRQGAY KAVKALREAG YLSEGPVIKL 

        70         80         90        100        110        120 
TQKGRDALSI VLRNLLRYFD IASIKLVGRV VTGLGEGAFY MSLEGYRRAI ERELGFTPYP 

       130        140        150        160        170        180 
GTLNIKLEPQ SLAHRRYLDG LPGIHIPGFT NGMRTYGAVK AFRARLADVE GAVVMPERTH 

       190        200        210 
HPVDVIEFIA PVRVRDVLGL KDGDRVELEV YL 

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References

[1]"Complete sequence of Pyrobaculum calidifontis JCM 11548."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 11548 / VA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000561 Genomic DNA. Translation: ABO08496.1.
RefSeqYP_001055962.1. NC_009073.1.

3D structure databases

ProteinModelPortalA3MV29.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3MV29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4909736.
GenomeReviewsGene locus Pcal_1071 in contig CP000561_GR.
KEGGpcl:Pcal_1071.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG10832.
HOGENOMHBG553349.
OMAMPERTHH.
ProtClustDBCLSK631895.

Family and domain databases

HAMAPMF_01285. Riboflavin_kinase. Fused.
[Tree]
InterProIPR023470. Riboflavin_kinase_archaeal.
IPR023602. Riboflavin_kinase_CTP-dep.
IPR023465. Riboflavin_kinase_domain.
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIFK_PYRCJ
AccessionPrimary (citable) accession number: A3MV29
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: April 3, 2007
Last modified: January 25, 2012
This is version 35 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