ID A0AAE1M468_9HYPO Unreviewed; 581 AA.
AC A0AAE1M468;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE RecName: Full=Dihydroxyacetone kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Triagg1_1400 {ECO:0000313|EMBL:KAK4083738.1};
OS Trichoderma aggressivum f. europaeum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=173218 {ECO:0000313|EMBL:KAK4083738.1, ECO:0000313|Proteomes:UP001273209};
RN [1] {ECO:0000313|EMBL:KAK4083738.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 100526 {ECO:0000313|EMBL:KAK4083738.1};
RA Beijen E., Ohm R.A.;
RT "The genome sequences of three competitors of mushroom-forming fungi.";
RL Submitted (NOV-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of
CC glyceraldehyde. {ECO:0000256|ARBA:ARBA00003264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde + ATP = D-glyceraldehyde 3-phosphate + ADP +
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; Evidence={ECO:0000256|ARBA:ARBA00047974};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone + ATP = dihydroxyacetone phosphate + ADP +
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; Evidence={ECO:0000256|ARBA:ARBA00048898};
CC -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC from glycerol (oxidative route): step 2/2.
CC {ECO:0000256|ARBA:ARBA00004778}.
CC -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC {ECO:0000256|ARBA:ARBA00008757}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK4083738.1}.
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DR EMBL; JAWRVG010000003; KAK4083738.1; -; Genomic_DNA.
DR RefSeq; XP_062759739.1; XM_062895467.1.
DR AlphaFoldDB; A0AAE1M468; -.
DR GeneID; 87915372; -.
DR Proteomes; UP001273209; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0019563; P:glycerol catabolic process; IEA:TreeGrafter.
DR FunFam; 3.40.50.10440:FF:000002; Dihydroxyacetone kinase; 1.
DR FunFam; 1.25.40.340:FF:000001; Dihydroxyacetone kinase 1; 1.
DR FunFam; 3.30.1180.20:FF:000001; Dihydroxyacetone kinase 1; 1.
DR Gene3D; 1.25.40.340; -; 1.
DR Gene3D; 3.40.50.10440; Dihydroxyacetone kinase, domain 1; 1.
DR Gene3D; 3.30.1180.20; Dihydroxyacetone kinase, domain 2; 1.
DR InterPro; IPR012734; DhaK_ATP.
DR InterPro; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR InterPro; IPR050861; Dihydroxyacetone_Kinase.
DR NCBIfam; TIGR02361; dak_ATP; 1.
DR PANTHER; PTHR28629:SF14; DIHYDROXYACETONE KINASE 1; 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 {ECO:0000256|ARBA:ARBA00022840};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP001273209};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..347
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 384..580
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT ACT_SITE 224
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 56..59
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 581 AA; 60653 MW; 26EFED5E72141B4C CRC64;
MSSKHFVNDP TKLVNDALLG ITLANPAVAL DTDNKTIYRR LNLNGSSQVS LLSGGGSGHE
PSFAAFVGNG LLSAAVAGTI FASPNTEQVR RAIMGLVDST RGVLVIVMNY TGDVLNFGVA
VEQAKSAGLD VEMLVVADDV GVGRQRAGKV GRRGIAGTVL VQKIAGALAA QGADLAEVHR
IGRLAADNLV SVGASLEHVH VPGHAAHGDD GLQLGEVELG MGIHNEPGSG RRTADLPELV
AAMLAQLLDE NDKDRAFLSI KSSDEVVLLV NNLGGVSVLE MGAITTEVVT QLKGQYDIRP
VRVLSGTYMT SLNGLGFSIS LLKVVDTGIY GSAMVQLLDA PSEATGWFAP ISTQTWEAKV
QSTREYKEAP VRTVQATGLK LNPTAAKSAL VRALERVVAS EPEITKYDQV VGDGDCGFGL
KRGAEAILTF LSRREFSGDA VIDAADIVPL VEKTMDGTSG ALYAIFLNAL VRSLAAAPPG
EATPQVWARA LEQSSAAMSK YTSARPGDRT LVDALYPFIE MLGKTGDVKK AAEAASIGAE
KTKGMKASLG RTVYVGGTGF QECPDPGAWG LRAFFLGLAG A
//
