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Database: UniProt
Entry: DAK2_YEAST
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ID   DAK2_YEAST              Reviewed;         591 AA.
AC   P43550; D6VTH7;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-NOV-2023, entry version 168.
DE   RecName: Full=Dihydroxyacetone kinase 2;
DE            Short=DHA kinase 2;
DE            EC=2.7.1.28;
DE            EC=2.7.1.29;
DE   AltName: Full=Glycerone kinase 2;
DE   AltName: Full=Triokinase 2;
DE   AltName: Full=Triose kinase 2;
GN   Name=DAK2; OrderedLocusNames=YFL053W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA   Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA   Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT   cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
CC   -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of
CC       glyceraldehyde. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate +
CC         H(+); Xref=Rhea:RHEA:15773, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57642, ChEBI:CHEBI:456216;
CC         EC=2.7.1.29;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate +
CC         H(+); Xref=Rhea:RHEA:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:59776, ChEBI:CHEBI:456216;
CC         EC=2.7.1.28;
CC   -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC       from glycerol (oxidative route): step 2/2.
CC   -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC       {ECO:0000305}.
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DR   EMBL; D50617; BAA09188.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12387.1; -; Genomic_DNA.
DR   PIR; S56202; S56202.
DR   RefSeq; NP_116602.1; NM_001179914.1.
DR   AlphaFoldDB; P43550; -.
DR   SMR; P43550; -.
DR   BioGRID; 31094; 41.
DR   DIP; DIP-6539N; -.
DR   IntAct; P43550; 2.
DR   MINT; P43550; -.
DR   STRING; 4932.YFL053W; -.
DR   iPTMnet; P43550; -.
DR   PaxDb; 4932-YFL053W; -.
DR   PeptideAtlas; P43550; -.
DR   EnsemblFungi; YFL053W_mRNA; YFL053W; YFL053W.
DR   GeneID; 850491; -.
DR   KEGG; sce:YFL053W; -.
DR   AGR; SGD:S000001841; -.
DR   SGD; S000001841; DAK2.
DR   VEuPathDB; FungiDB:YFL053W; -.
DR   eggNOG; KOG2426; Eukaryota.
DR   GeneTree; ENSGT00390000015415; -.
DR   HOGENOM; CLU_017054_6_0_1; -.
DR   InParanoid; P43550; -.
DR   OMA; CGLCLKT; -.
DR   OrthoDB; 6043at2759; -.
DR   BioCyc; MetaCyc:YFL053W-MONOMER; -.
DR   BioCyc; YEAST:YFL053W-MONOMER; -.
DR   BRENDA; 2.7.1.29; 984.
DR   UniPathway; UPA00617; UER00669.
DR   BioGRID-ORCS; 850491; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P43550; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43550; Protein.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004371; F:glycerone kinase activity; IMP:SGD.
DR   GO; GO:0050354; F:triokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019588; P:anaerobic glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR   GO; GO:0061610; P:glycerol to glycerone phosphate metabolic process; IGI:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.340; -; 1.
DR   InterPro; IPR012734; DhaK_ATP.
DR   InterPro; IPR004006; DhaK_dom.
DR   InterPro; IPR004007; DhaL_dom.
DR   InterPro; IPR036117; DhaL_dom_sf.
DR   NCBIfam; TIGR02361; dak_ATP; 1.
DR   PANTHER; PTHR28629:SF12; DIHYDROXYACETONE KINASE 2; 1.
DR   PANTHER; PTHR28629; TRIOKINASE/FMN CYCLASE; 1.
DR   Pfam; PF02733; Dak1; 1.
DR   Pfam; PF02734; Dak2; 1.
DR   SMART; SM01120; Dak2; 1.
DR   SUPFAM; SSF82549; DAK1/DegV-like; 1.
DR   SUPFAM; SSF101473; DhaL-like; 1.
DR   PROSITE; PS51481; DHAK; 1.
DR   PROSITE; PS51480; DHAL; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..591
FT                   /note="Dihydroxyacetone kinase 2"
FT                   /id="PRO_0000121523"
FT   DOMAIN          8..344
FT                   /note="DhaK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT   DOMAIN          384..587
FT                   /note="DhaL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT   REGION          40..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        223
FT                   /note="Tele-hemiaminal-histidine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT   BINDING         58..61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         413..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         459..460
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         511..512
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         572..574
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   591 AA;  62135 MW;  EE317EC120C0E313 CRC64;
     MSHKQFKSDG NIVTPYLLGL ARSNPGLTVI KHDRVVFRTA SAPNSGNPPK VSLVSGGGSG
     HEPTHAGFVG EGALDAIAAG AIFASPSTKQ IYSAIKAVES PKGTLIIVKN YTGDIIHFGL
     AAERAKAAGM KVELVAVGDD VSVGKKKGSL VGRRGLGATV LVHKIAGAAA SHGLELAEVA
     EVAQSVVDNS VTIAASLDHC TVPGHKPEAI LGENEYEIGM GIHNESGTYK SSPLPSISEL
     VSQMLPLLLD EDEDRSYVKF EPKEDVVLMV NNMGGMSNLE LGYAAEVISE QLIDKYQIVP
     KRTITGAFIT ALNGPGFGIT LMNASKAGGD ILKYFDYPTT ASGWNQMYHS AKDWEVLAKG
     QVPTAPSLKT LRNEKGSGVK ADYDTFAKIL LAGIAKINEV EPKVTWYDTI AGDGDCGTTL
     VSGGEALEEA IKNHTLRLED AALGIEDIAY MVEDSMGGTS GGLYSIYLSA LAQGVRDSGD
     KELTAETFKK ASNVALDALY KYTRARPGYR TLIDALQPFV EALKAGKGPR AAAQAAYDGA
     EKTRKMDALV GRASYVAKEE LRKLDSEGGL PDPGAVGLAA LLDGFVTAAG Y
//
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