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Database: UniProt
Entry: A0A428TKS4_9HYPO
LinkDB: A0A428TKS4_9HYPO
Original site: A0A428TKS4_9HYPO 
ID   A0A428TKS4_9HYPO        Unreviewed;       591 AA.
AC   A0A428TKS4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Dihydroxyacetone kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CEP52_007868 {ECO:0000313|EMBL:RSM02633.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSM02633.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSM02633.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSM02633.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) 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=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:RSM02633.1}.
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DR   EMBL; NKCK01000074; RSM02633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428TKS4; -.
DR   STRING; 1325735.A0A428TKS4; -.
DR   UniPathway; UPA00617; UER00669.
DR   Proteomes; UP000287144; 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:SF14; CHROMOSOME 1, WHOLE GENOME SHOTGUN SEQUENCE; 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:UP000287144};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..349
FT                   /note="DhaK"
FT                   /evidence="ECO:0000259|PROSITE:PS51481"
FT   DOMAIN          385..585
FT                   /note="DhaL"
FT                   /evidence="ECO:0000259|PROSITE:PS51480"
FT   ACT_SITE        218
FT                   /note="Tele-hemiaminal-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT   BINDING         54..57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ   SEQUENCE   591 AA;  63030 MW;  8E1E6B09A6D092CB CRC64;
     MSTRHLFDSP EGLVNKALRG IISYNTSLRL DETNRVVYDT EHRRSNVSIV SGGGSGHEPA
     WTGYVGKNML AASVQGDIFA SPSTKQILAA IEAVPSDEGT ILVITNYTGD CLHFGLANEK
     AIARGHRCRM IICGDDVSVG RRGGIVGRRG LAGQIGVLKV MGGAAGAGHS LDDVYNLGVA
     FSEQIVSIAA TLDHCHVPGR SQHGALAVNE IELGTGPHNE PGYMKLSPAP TTPELVRQIL
     KHCLDENDPT RGYVKFAPKD KTILLISNFG GISHLELGAL LDEVLEQLAN EWGIEPSRTC
     AGFLETSLNA PAFSVSVINV SAAARNCRYS ADRILDFFDT KTNTFWESMA GSQTRRCSRK
     EQLVHPPKEA EKIINDETDL KIDATILEKM LRSACDAIIQ AEPHLTKWDT VMGDGDCGET
     LKTGATSLIQ ALDKGLARSG SVVAVLQELE DIVESKMGGT LGGILGIFFV SLRTAVEKNS
     HIARSNGPIA LWSEALSLAL ENLSRYTPAK VGDRTVMDTL IPFAEIIAKA GFVGGVEAAV
     QGAEATKTMK PRLGRATYVG VGDSTELPPD PGAWGAMVAI RGLHSGLEVI T
//
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