DAK_PICAN
ID DAK_PICAN Reviewed; 609 AA.
AC O60017;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Dihydroxyacetone kinase;
DE Short=DHA kinase;
DE EC=2.7.1.28;
DE EC=2.7.1.29;
DE AltName: Full=Glycerone kinase;
DE AltName: Full=Triokinase;
DE AltName: Full=Triose kinase;
GN Name=DAK;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=9683670; DOI=10.1007/s002940050360;
RA van der Klei I.J., van der Heide M., Baerends R.J.S., Rechinger K.-B.,
RA Nicolay K., Kiel J.A.K.W., Veenhuis M.;
RT "The Hansenula polymorpha per6 mutant is affected in two adjacent genes
RT which encode dihydroxyacetone kinase and a novel protein, Pak1p, involved
RT in peroxisome integrity.";
RL Curr. Genet. 34:1-11(1998).
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; AY383554; AAC27705.1; -; Genomic_DNA.
DR AlphaFoldDB; O60017; -.
DR SMR; O60017; -.
DR BioCyc; MetaCyc:MON-13163; -.
DR UniPathway; UPA00617; UER00669.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:UniProtKB-EC.
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: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; Transferase.
FT CHAIN 1..609
FT /note="Dihydroxyacetone kinase"
FT /id="PRO_0000121518"
FT DOMAIN 8..355
FT /note="DhaK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT DOMAIN 392..600
FT /note="DhaL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT ACT_SITE 232
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT BINDING 53..56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 421..424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 467..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 523..524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 585..587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 609 AA; 65071 MW; 16A0CF4439C967AA CRC64;
MSSKHWNYKQ DLVHAHLKGL CHANPDLQFI ESERVVINKH SKPDKVMILS GGGSGHEPLH
AGFVGEGCLD VGVAGFVFAS PSTKQIVSGL KAKPSDKGTL IVVKNYTGDI LHFGLAAERA
KAEGVPVELL IVQDDVSVGR TKNGMVGRRG LAGTSLVHKI VGAKAAKDSN KASLSEVYQL
GEAVVANLVT IGASLDHCTI PGNRHHESES DDEDEQKHLL KEDEIEVGMG IHNESGIKRV
SPIPTIDTLV ADLLKYLLDK SDEERHYVDF DSSDEVVLMI NNLGGTSNLE LYAIQNTVVE
QLATDYKIKP ARVYTGAYTT SLDGPGFSIT LLNVTRAGGK EVFDCLDYPT KVPGWNSSYT
TAEWAAKSES FVIDAPPVSD ASATSKVRFS SSTVKAVLES GCKKLLTKEP KITLYDTVAG
DGDCGETLAN GAHAILDLLA ADKLEITDGV RSLTQITDVV ETAMGGTSGG LYSIFISALA
KSLKDRELQQ GGYEVTPQIL AASLKDALES LYRYTRARAG DRTLIDALAP FVEQFAASKG
DLNQANKACH EGAESTRKLK AKFGRASYVS EEEFKPFEAE GGLPDPGAIG LAALVDGFAE
AYSKIGSNL
