DAK2_YEAST
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 03-AUG-2022, entry version 162.
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; 40.
DR DIP; DIP-6539N; -.
DR IntAct; P43550; 2.
DR MINT; P43550; -.
DR STRING; 4932.YFL053W; -.
DR iPTMnet; P43550; -.
DR PaxDb; P43550; -.
DR PRIDE; P43550; -.
DR EnsemblFungi; YFL053W_mRNA; YFL053W; YFL053W.
DR GeneID; 850491; -.
DR KEGG; sce:YFL053W; -.
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; EPKITHY; -.
DR BioCyc; MetaCyc:YFL053W-MON; -.
DR BioCyc; YEAST:YFL053W-MON; -.
DR BRENDA; 2.7.1.29; 984.
DR UniPathway; UPA00617; UER00669.
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:0097237; P:cellular response to toxic substance; IMP:SGD.
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 Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF101473; SSF101473; 1.
DR TIGRFAMs; TIGR02361; dak_ATP; 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
