Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8VC30 (DHAK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)

Including the following 2 domains:

  1. ATP-dependent dihydroxyacetone kinase
    Short name=DHA kinase
    EC=2.7.1.28
    EC=2.7.1.29
    Alternative name(s):
    Glycerone kinase
    Triokinase
    Triose kinase
  2. FAD-AMP lyase (cyclizing)
    EC=4.6.1.15
    Alternative name(s):
    FAD-AMP lyase (cyclic FMN forming)
    FMN cyclase
Gene names
Name:Dak
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate By similarity.

Catalytic activity

ATP + glycerone = ADP + glycerone phosphate.

ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate.

FAD = AMP + riboflavin cyclic-4',5'-phosphate.

Cofactor

Magnesium By similarity.

Manganese or cobalt; for FAD-AMP lyase activity By similarity.

Enzyme regulation

Each activity is inhibited by the substrate(s) of the other By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the dihydroxyacetone kinase (DAK) family.

Contains 1 DhaK domain.

Contains 1 DhaL domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 578578Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)
PRO_0000121526

Regions

Domain9 – 336328DhaK
Domain372 – 571200DhaL
Nucleotide binding401 – 4044ATP By similarity
Nucleotide binding446 – 4472ATP By similarity
Nucleotide binding494 – 4952ATP By similarity
Nucleotide binding556 – 5583ATP By similarity
Region56 – 594Dihydroxyacetone binding By similarity

Sites

Active site2211Tele-hemiaminal-histidine intermediate By similarity
Binding site1091Dihydroxyacetone By similarity
Binding site1141Dihydroxyacetone By similarity
Binding site4861ATP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VC30 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 5C6FCABDD6F2EF2A

FASTA57859,691
        10         20         30         40         50         60 
MSSKKMVNSV EGCADDALAG LVASNPDLQL LQGHRVALRS DLDTLKGRVA LLSGGGSGHE 

        70         80         90        100        110        120 
PAHAGFIGKG MLTGVIAGSV FASPPVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL 

       130        140        150        160        170        180 
AMEQAKAEGI SVEMVIVEDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEE GMGLEEITKR 

       190        200        210        220        230        240 
VSVIAKTMGT LGVSLSSCSV PGATHTFELA ADEIELGLGI HGEAGVRRIK IAPVDQIVTL 

       250        260        270        280        290        300 
MLDHMTNTSN IFHVPVRSGS SVVLIVNNLG GLSFLELGII ADAAIRLLEG RGVKVARALV 

       310        320        330        340        350        360 
GTFMSALEMP GVSLTLMLVD EPVLKLIDAE TTAKAWPHMA KVSVTGRKRI RAAPTEPPEA 

       370        380        390        400        410        420 
PEATAAGGVT SKQMALVLDR ICTTLIGLEE HLNALDRAAG DGDCGSTHSR AAKAIQGWLK 

       430        440        450        460        470        480 
EGPSLTSPAQ VLSRLSVLLL ERMGGSSGAL YGLFLTAAAQ PLKAKTDLPT WSAAMDAGLE 

       490        500        510        520        530        540 
SMQKYGKAAP GDRTMLDSLW AAAQEFQAWK SPGASLLPVL TKAVKSAEAA AEATKNMEAG 

       550        560        570 
AGRASYISSA QLDQPDPGAV AAAAIFRAIL EVLQTQGA

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC021917 mRNA. Translation: AAH21917.1.
IPIIPI00310669.
RefSeqNP_663471.1. NM_145496.1.
UniGeneMm.374868.

3D structure databases

ProteinModelPortalQ8VC30.
SMRQ8VC30. Positions 3-571.
ModBaseSearch...

PTM databases

PhosphoSiteQ8VC30.

2D gel databases

REPRODUCTION-2DPAGEIPI00310669.
Q8VC30.

Proteomic databases

PaxDbQ8VC30.
PRIDEQ8VC30.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037678; ENSMUSP00000044556; ENSMUSG00000034371.
GeneID225913.
KEGGmmu:225913.
UCSCuc008gql.1. mouse.

Organism-specific databases

CTD26007.
MGIMGI:2385084. Dak.

Phylogenomic databases

eggNOGCOG2376.
GeneTreeENSGT00390000015415.
HOGENOMHOG000234158.
HOVERGENHBG079502.
InParanoidQ8VC30.
KOK00863.
OMATLMLDHM.
OrthoDBEOG4PRSQT.

Gene expression databases

BgeeQ8VC30.
CleanExMM_DAK.
GenevestigatorQ8VC30.
GermOnlineENSMUSG00000034371. Mus musculus.

Family and domain databases

InterProIPR004006. Dak1.
IPR004007. Dak2.
IPR012734. DhaK_ATP.
[Graphical view]
PfamPF02733. Dak1. 1 hit.
PF02734. Dak2. 1 hit.
[Graphical view]
SUPFAMSSF101473. Dak2. 1 hit.
TIGRFAMsTIGR02361. dak_ATP. 1 hit.
PROSITEPS51481. DHAK. 1 hit.
PS51480. DHAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio377881.
SOURCESearch...

Entry information

Entry nameDHAK_MOUSE
AccessionPrimary (citable) accession number: Q8VC30
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2002
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents