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Database: UniProt
Entry: A0A0F9ZBW7_TRIHA
LinkDB: A0A0F9ZBW7_TRIHA
Original site: A0A0F9ZBW7_TRIHA 
ID   A0A0F9ZBW7_TRIHA        Unreviewed;       567 AA.
AC   A0A0F9ZBW7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Dihydroxyacetone kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=THAR02_09925 {ECO:0000313|EMBL:KKO97976.1};
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544 {ECO:0000313|EMBL:KKO97976.1, ECO:0000313|Proteomes:UP000034112};
RN   [1] {ECO:0000313|Proteomes:UP000034112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX   PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA   Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA   Pe M.E., Sarrocco S., Vannacci G.;
RT   "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT   T6776.";
RL   Genome Announc. 3:E0064715-E0064715(2015).
CC   -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of
CC       glyceraldehyde. {ECO:0000256|ARBA:ARBA00003264}.
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; Evidence={ECO:0000256|ARBA:ARBA00000031};
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; Evidence={ECO:0000256|ARBA:ARBA00001015};
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:KKO97976.1}.
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DR   EMBL; JOKZ01000479; KKO97976.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F9ZBW7; -.
DR   OMA; QCDIENK; -.
DR   OrthoDB; 6043at2759; -.
DR   UniPathway; UPA00617; UER00669.
DR   Proteomes; UP000034112; Unassembled WGS sequence.
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   NCBIfam; TIGR02361; dak_ATP; 1.
DR   PANTHER; PTHR28629; TRIOKINASE/FMN CYCLASE; 1.
DR   PANTHER; PTHR28629:SF4; 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:UP000034112};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..347
FT                   /note="DhaK"
FT                   /evidence="ECO:0000259|PROSITE:PS51481"
FT   DOMAIN          384..566
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   567 AA;  59297 MW;  EA8A9A7B71FB98C8 CRC64;
     MSSKHFVNDP TKLVNDALFG ITLANPAIAL DADNKTIYRR PNLNGSSQVS LLSGGGSGHE
     PSFAAFVGDG LLSAAVAGTI FASPNTEQVR KAIMGLVDST RGVLVIVMNY TGDVLNFGVA
     IEQAKSAGLN VEMLVVADDV GVGRQRAGKV GRRGIAGTVL VQKIAGALAA QGTDLAEVHR
     IGRLAADNLV SVGASLEHVH VPGHAAHGDN GLQIGEVELG MGIHNEPGSG RHTADLPELV
     TAMLSQLLDE NDKDRAFLSI KPSDEVVLLV NNLGGVSVLE MGAITTEVVT QLKGQYDIRP
     VRILSGTYMT SLNGLGFSIS LLKVVDTGIN GFTMIQLLDA PSEATGWSAP ISTPTWEAKI
     QSTREYKEAP VKTVQATGLK LNPAAAKSAL VRALERVVAS EPEITKYDEI VGDGDCGFGL
     KRGAEAILTF LSTRDFSGDA VVDVADIVPL VEKTMDVRSL AASPPGEATP QVWAKALEQS
     SAAMSKYTSA RPGDRTLVDA LYPFIETLTK TGDVKEAAKA ASIGAEKTKG MRASLGRTVY
     VGGTGFQECP DPGAWGLRSF FLGLAGI
//
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