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A2STY4 (RIFK_METLZ) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 37. 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:Mlab_1629
OrganismMethanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z) [Complete proteome] [HAMAP]
Taxonomic identifier410358 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanocorpusculaceaeMethanocorpusculum

Protein attributes

Sequence length222 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 – 222222Riboflavin kinase HAMAP MF_01285
PRO_0000322092

Regions

Nucleotide binding104 – 1096CDP By similarity
Nucleotide binding203 – 2064CDP By similarity
Region1 – 9494H-T-H motif-like HAMAP MF_01285
Region95 – 222128Riboflavin kinase HAMAP MF_01285

Sites

Metal binding1331Magnesium By similarity
Metal binding1351Magnesium By similarity
Binding site1901FMN By similarity
Binding site1981FMN By similarity

Sequences

Sequence LengthMass (Da)Tools
A2STY4 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 8766FBD0417E1459

FASTA22224,735
        10         20         30         40         50         60 
METIDAEDAA CLRRIALLGG CKGPVRLSTQ ALGDQLGISQ QTASRRLQSL EKAQMISRTA 

        70         80         90        100        110        120 
ESTGQYVLVT RSGEEHLRRE FAEYAKIFDV KDEQYVLTGT VMSGVGEGRY YMSIPHYQEQ 

       130        140        150        160        170        180 
FEKLCGFTPY PGTLNIKLNP QSVLIRKRMD SLEWTIVPGF KDEHRMFGEA RCIKCTISGI 

       190        200        210        220 
PCAIVVPGRT HHPEEVIEVI SGTQLRDALD LTENSEVVVV IG 

« Hide

References

[1]"Complete genome sequence of Methanocorpusculum labreanum type strain Z."
Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L., Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:197-203(2009) [PubMed: 21304657] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43576 / DSM 4855 / Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000559 Genomic DNA. Translation: ABN07790.1.
RefSeqYP_001031057.1. NC_008942.1.

3D structure databases

ProteinModelPortalA2STY4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2STY4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4795257.
GenomeReviewsGene locus Mlab_1629 in contig CP000559_GR.
KEGGmla:Mlab_1629.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG10832.
HOGENOMHBG553349.
OMAGRHYISL.
ProtClustDBCLSK949639.

Enzyme and pathway databases

BioCycMLAB410358:MLAB_1629-MONOMER.

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_METLZ
AccessionPrimary (citable) accession number: A2STY4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 6, 2007
Last modified: November 16, 2011
This is version 37 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