ID   DAK_PICPA               Reviewed;         608 AA.
AC   O74192;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 86.
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   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9675820;
RX   DOI=10.1002/(sici)1097-0061(19980615)14:8<759::aid-yea275>3.0.co;2-a;
RA   Luers G.H., Advani R., Wenzel T., Subramani S.;
RT   "The Pichia pastoris dihydroxyacetone kinase is a PTS1-containing, but
RT   cytosolic, protein that is essential for growth on methanol.";
RL   Yeast 14:759-771(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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC       {ECO:0000305}.
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DR   EMBL; AF019198; AAC39490.1; -; Genomic_DNA.
DR   AlphaFoldDB; O74192; -.
DR   SMR; O74192; -.
DR   BRENDA; 2.7.1.29; 4827.
DR   UniPathway; UPA00617; UER00669.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; Cytoplasm; Glycerol metabolism; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..608
FT                   /note="Dihydroxyacetone kinase"
FT                   /id="PRO_0000121519"
FT   DOMAIN          8..357
FT                   /note="DhaK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT   DOMAIN          392..599
FT                   /note="DhaL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT   ACT_SITE        234
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         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
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         584..586
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   608 AA;  65312 MW;  412F00BA4D965119 CRC64;
     MSSKHWDYKK DLVLSHLAGL CQSNPHVRLI ESERVVISAE NQEDKITLIS GGGSGHEPLH
     AGFVTKDGLL DAAVAGFIFA SPSTKQIFSA IKAKPSKKGT LIIVKNYTGD ILHFGLAAEK
     AKAEGLNAEL LIVQDDVSVG KAKNGLVGRR GLAGTSLVHK ILGAKAYLQK DNLELHQLVT
     FGEKVVANLV TIGASLDHVT IPARANKQEE DDSDDEHGYE VLKHDEFEIG MGIHNEPGIK
     KSSPIPTVDE LVAELLEYLL STTDKDRNYV QFDKNDEVVL LINNLGGTSV LELYAIQNIV
     VDQLASKYSI KPVRIFTGTF TTSLDGPGFS ITLLNATKTG DKDILKFLDH KTSAPGWNSN
     ISDWSGRVDN FIVAAPEIDE GDSSSKVSVD AKLYADLLES GVKKVISKEP KITLYDTVAG
     DGDCGETLAN GSNAILKALA EGKLDLKDGV KSLVQITDIV ETAMGGTSGG LYSIFISALA
     KSLKEKELSE GAYTLTLETI SGSLQAALQS LFKYTRARTG DRTLIDALEP FVKEFAKSKD
     LKLANKAAHD GAEATRKLEA KFGRASYVAE EEFKQFESEG GLPDPGAIGL AALISGITDA
     YFKSETKL