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Protein

Dihydroxyacetone kinase 1

Gene

DAK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.By similarity

Catalytic activityi

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

Pathwayi: glycerol fermentation

This protein is involved in step 2 of the subpathway that synthesizes glycerone phosphate from glycerol (oxidative route).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Dihydroxyacetone kinase 2 (DAK2), Dihydroxyacetone kinase 1 (DAK1)
This subpathway is part of the pathway glycerol fermentation, which is itself part of Polyol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycerone phosphate from glycerol (oxidative route), the pathway glycerol fermentation and in Polyol metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031SubstrateBy similarity
Binding sitei108 – 1081SubstrateBy similarity
Active sitei220 – 2201Tele-hemiaminal-histidine intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi415 – 4184ATPBy similarity
Nucleotide bindingi459 – 4602ATPBy similarity
Nucleotide bindingi514 – 5152ATPBy similarity
Nucleotide bindingi567 – 5693ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glycerone kinase activity Source: SGD
  • triokinase activity Source: UniProtKB-EC

GO - Biological processi

  • anaerobic glycerol catabolic process Source: UniProtKB-UniPathway
  • cellular response to toxic substance Source: SGD
  • glycerol catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycerol metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16994.
YEAST:YML070W-MONOMER.
BRENDAi2.7.1.29. 984.
ReactomeiR-SCE-70350. Fructose catabolism.
UniPathwayiUPA00617; UER00669.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroxyacetone kinase 1 (EC:2.7.1.28, EC:2.7.1.29)
Short name:
DHA kinase 1
Alternative name(s):
Glycerone kinase 1
Triokinase 1
Triose kinase 1
Gene namesi
Name:DAK1
Ordered Locus Names:YML070W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML070W.
SGDiS000004535. DAK1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 584583Dihydroxyacetone kinase 1PRO_0000121522Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei5 – 51PhosphoserineCombined sources
Modified residuei365 – 3651PhosphoserineCombined sources
Modified residuei512 – 5121PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP54838.

PTM databases

iPTMnetiP54838.

Interactioni

Protein-protein interaction databases

BioGridi35096. 38 interactions.
DIPiDIP-4531N.
IntActiP54838. 2 interactions.
MINTiMINT-478762.

Structurei

3D structure databases

ProteinModelPortaliP54838.
SMRiP54838. Positions 7-583.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 353347DhaKPROSITE-ProRule annotationAdd
BLAST
Domaini386 – 582197DhaLPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 544Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 DhaK domain.PROSITE-ProRule annotation
Contains 1 DhaL domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000015415.
HOGENOMiHOG000234158.
InParanoidiP54838.
KOiK00863.
OMAiEHVHIPG.
OrthoDBiEOG74XSGF.

Family and domain databases

InterProiIPR012734. DhaK_ATP.
IPR004006. DhaK_dom.
IPR004007. DhaL_dom.
[Graphical view]
PfamiPF02733. Dak1. 1 hit.
PF02734. Dak2. 1 hit.
[Graphical view]
SMARTiSM01120. Dak2. 1 hit.
[Graphical view]
SUPFAMiSSF101473. SSF101473. 1 hit.
TIGRFAMsiTIGR02361. dak_ATP. 1 hit.
PROSITEiPS51481. DHAK. 1 hit.
PS51480. DHAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54838-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAKSFEVTD PVNSSLKGFA LANPSITLVP EEKILFRKTD SDKIALISGG
60 70 80 90 100
GSGHEPTHAG FIGKGMLSGA VVGEIFASPS TKQILNAIRL VNENASGVLL
110 120 130 140 150
IVKNYTGDVL HFGLSAERAR ALGINCRVAV IGDDVAVGRE KGGMVGRRAL
160 170 180 190 200
AGTVLVHKIV GAFAEEYSSK YGLDGTAKVA KIINDNLVTI GSSLDHCKVP
210 220 230 240 250
GRKFESELNE KQMELGMGIH NEPGVKVLDP IPSTEDLISK YMLPKLLDPN
260 270 280 290 300
DKDRAFVKFD EDDEVVLLVN NLGGVSNFVI SSITSKTTDF LKENYNITPV
310 320 330 340 350
QTIAGTLMTS FNGNGFSITL LNATKATKAL QSDFEEIKSV LDLLNAFTNA
360 370 380 390 400
PGWPIADFEK TSAPSVNDDL LHNEVTAKAV GTYDFDKFAE WMKSGAEQVI
410 420 430 440 450
KSEPHITELD NQVGDGDCGY TLVAGVKGIT ENLDKLSKDS LSQAVAQISD
460 470 480 490 500
FIEGSMGGTS GGLYSILLSG FSHGLIQVCK SKDEPVTKEI VAKSLGIALD
510 520 530 540 550
TLYKYTKARK GSSTMIDALE PFVKEFTASK DFNKAVKAAE EGAKSTATFE
560 570 580
AKFGRASYVG DSSQVEDPGA VGLCEFLKGV QSAL
Length:584
Mass (Da):62,207
Last modified:October 1, 1996 - v1
Checksum:i3B488A5649FAFE25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38114 Genomic DNA. Translation: CAA86250.1.
BK006946 Genomic DNA. Translation: DAA09827.1.
PIRiS48327.
RefSeqiNP_013641.1. NM_001182429.1.

Genome annotation databases

EnsemblFungiiYML070W; YML070W; YML070W.
GeneIDi854932.
KEGGisce:YML070W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38114 Genomic DNA. Translation: CAA86250.1.
BK006946 Genomic DNA. Translation: DAA09827.1.
PIRiS48327.
RefSeqiNP_013641.1. NM_001182429.1.

3D structure databases

ProteinModelPortaliP54838.
SMRiP54838. Positions 7-583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35096. 38 interactions.
DIPiDIP-4531N.
IntActiP54838. 2 interactions.
MINTiMINT-478762.

PTM databases

iPTMnetiP54838.

Proteomic databases

MaxQBiP54838.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML070W; YML070W; YML070W.
GeneIDi854932.
KEGGisce:YML070W.

Organism-specific databases

EuPathDBiFungiDB:YML070W.
SGDiS000004535. DAK1.

Phylogenomic databases

GeneTreeiENSGT00390000015415.
HOGENOMiHOG000234158.
InParanoidiP54838.
KOiK00863.
OMAiEHVHIPG.
OrthoDBiEOG74XSGF.

Enzyme and pathway databases

UniPathwayiUPA00617; UER00669.
BioCyciMetaCyc:MONOMER-16994.
YEAST:YML070W-MONOMER.
BRENDAi2.7.1.29. 984.
ReactomeiR-SCE-70350. Fructose catabolism.

Miscellaneous databases

PROiP54838.

Family and domain databases

InterProiIPR012734. DhaK_ATP.
IPR004006. DhaK_dom.
IPR004007. DhaL_dom.
[Graphical view]
PfamiPF02733. Dak1. 1 hit.
PF02734. Dak2. 1 hit.
[Graphical view]
SMARTiSM01120. Dak2. 1 hit.
[Graphical view]
SUPFAMiSSF101473. SSF101473. 1 hit.
TIGRFAMsiTIGR02361. dak_ATP. 1 hit.
PROSITEiPS51481. DHAK. 1 hit.
PS51480. DHAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway."
    Norbeck J., Blomberg A.
    J. Biol. Chem. 272:5544-5554(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 104-112 AND 159-167, PARTIAL CHARACTERIZATION.
    Strain: ATCC 44827 / SKQ2N.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDAK1_YEAST
AccessioniPrimary (citable) accession number: P54838
Secondary accession number(s): D6VZA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 23600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.