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Q4KLZ6 (DHAK_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.2

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. Ref.3

Manganese or cobalt; for FAD-AMP lyase activity. Ref.3

Enzyme regulation

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

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the dihydroxyacetone kinase (DAK) family.

Contains 1 DhaK domain.

Contains 1 DhaL domain.

Biophysicochemical properties

Kinetic parameters:

KM=8.8 µM for FAD with manganese Ref.3

KM=12.5 µM for ADP-glucose with manganese

KM=652 µM for UDP-glucose with manganese

KM=606 µM for UDP-galactose with manganese

KM=714 µM for UDP-xylose with manganese

KM=107 µM for UDP-glucuronate with manganese

KM=108 µM for UDP-galacturonate with manganese

KM=416 µM for CDP-glucose with manganese

KM=795 µM for CDP-glycerol with manganese

KM=784 µM for GDP-glucose with manganese

KM=343 µM for GDP-alpha-L-fucose with manganese

KM=114 µM for FAD with cobalt

KM=120 µM for ADP-glucose with cobalt

KM=2550 µM for UDP-glucose with cobalt

KM=3661 µM for UDP-galactose with cobalt

KM=2354 µM for UDP-xylose with cobalt

KM=539 µM for UDP-glucuronate with cobalt

KM=759 µM for UDP-galacturonate with cobalt

KM=3703 µM for CDP-glucose with cobalt

KM=2031 µM for CDP-glycerol with cobalt

KM=2246 µM for GDP-glucose with cobalt

KM=991 µM for GDP-alpha-L-fucose with cobalt

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 578578Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)
PRO_0000121527

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
Q4KLZ6 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: C343482447F9770B

FASTA57859,444
        10         20         30         40         50         60 
MSSKKMVNSV EGCAGDALAG FVACNPDLQL LQGYRVALRS DLDSLKGRVA LLSGGGSGHE 

        70         80         90        100        110        120 
PAHAGFIGKG MLTGVIAGAV FASPAVGSIL AAIRAVAQAG TAGTLLIVKN YTGDRLNFGL 

       130        140        150        160        170        180 
AMEQAKAEGI SVEMVVIEDD SAFTVLKKAG RRGLCGTILI HKVAGALAEE GMGLEEITKK 

       190        200        210        220        230        240 
VSVIAKAIGT LGVSLSPCSV PGTKPTFELA ADEMELGLGI HGEAGVRRIK LVPVDQIVTL 

       250        260        270        280        290        300 
MLDHMTDTSN ISHVPVKSGS SVVLMVNNLG GLSFLELGII ADAAIRLLEG RGVKVARALV 

       310        320        330        340        350        360 
GTFMSALEMR GVSLTLMLVD EPLLKLIDAE TNAKAWPHMS KVSVTGRNRI RAAPTEPAEA 

       370        380        390        400        410        420 
PEATAAGGVA SKQMTLVLDR ISTTLIGLEE HLNALDRAAG DGDCGSTHSR AAKAIQGWLK 

       430        440        450        460        470        480 
EGPTPASPAQ VLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKANTDLPA WSAAMDAGLK 

       490        500        510        520        530        540 
AMQKYGKAAP GDRTMLDSLW AAAQELQAWK SPGASLLPVL TKAVKSAEAA AEATKNMEAG 

       550        560        570 
AGRASYISSA QLDQPDPGAV AAAAIFRAIL EVLQTKAA 

« Hide

References

« Hide 'large scale' 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].
Strain: Brown Norway.
Tissue: Testis.
[2]"Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases."
Cabezas A., Costas M.J., Pinto R.M., Couto A., Cameselle J.C.
Biochem. Biophys. Res. Commun. 338:1682-1689(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, FAD-AMP LYASE ACTIVITY.
[3]"Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): preference for FAD and specificity for splitting ribonucleoside diphosphate-X into ribonucleotide and a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion."
Cabezas A., Pinto R.M., Fraiz F., Canales J., Gonzalez-Santiago S., Cameselle J.C.
Biochemistry 40:13710-13722(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC098925 mRNA. Translation: AAH98925.1.
RefSeqNP_001034120.1. NM_001039031.1.
XP_006231118.1. XM_006231056.1.
XP_006231119.1. XM_006231057.1.
UniGeneRn.55630.

3D structure databases

ProteinModelPortalQ4KLZ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4580965.
STRING10116.ENSRNOP00000028102.

PTM databases

PhosphoSiteQ4KLZ6.

Proteomic databases

PaxDbQ4KLZ6.
PRIDEQ4KLZ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000028102; ENSRNOP00000028102; ENSRNOG00000020704.
GeneID361730.
KEGGrno:361730.
UCSCRGD:1311026. rat.

Organism-specific databases

CTD26007.
RGD1311026. Dak.

Phylogenomic databases

eggNOGCOG2376.
GeneTreeENSGT00390000015415.
HOGENOMHOG000234158.
HOVERGENHBG079502.
InParanoidQ4KLZ6.
KOK00863.
OMAKMEMVIV.
OrthoDBEOG71K630.
PhylomeDBQ4KLZ6.
TreeFamTF313821.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15866.

Gene expression databases

GenevestigatorQ4KLZ6.

Family and domain databases

InterProIPR004006. Dak1.
IPR012734. DhaK_ATP.
IPR004007. DhaL_dom.
[Graphical view]
PfamPF02733. Dak1. 1 hit.
PF02734. Dak2. 1 hit.
[Graphical view]
SUPFAMSSF101473. SSF101473. 1 hit.
TIGRFAMsTIGR02361. dak_ATP. 1 hit.
PROSITEPS51481. DHAK. 1 hit.
PS51480. DHAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio677430.
PROQ4KLZ6.

Entry information

Entry nameDHAK_RAT
AccessionPrimary (citable) accession number: Q4KLZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: August 2, 2005
Last modified: April 16, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families