ID A0A2T9XWW9_9FUNG Unreviewed; 596 AA.
AC A0A2T9XWW9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Dihydroxyacetone kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BB559_007561 {ECO:0000313|EMBL:PVU84565.1};
OS Furculomyces boomerangus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU84565.1, ECO:0000313|Proteomes:UP000245699};
RN [1] {ECO:0000313|EMBL:PVU84565.1, ECO:0000313|Proteomes:UP000245699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU84565.1,
RC ECO:0000313|Proteomes:UP000245699};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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:PVU84565.1}.
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DR EMBL; MBFT01001280; PVU84565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9XWW9; -.
DR STRING; 61424.A0A2T9XWW9; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000245699; 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; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
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:UP000245699};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..354
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 392..593
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
SQ SEQUENCE 596 AA; 63015 MW; 5882A24A0A1D4435 CRC64;
MVSEKHFVNN PSDLVKDSIL GLVSTSTHLK FDEESKVIYL RNIDDVKESQ VTLFCGGGAG
HEPAHGGFVG PSFLTSAVSG HVFASPSTSQ VLSCLQRTYS PNHGTIVIVK NYTGDILNFG
RAIERFKAEE AGKGSVDCKV SMVVVGDDVG VVNESEEIDV GRRGLSGTVL VNKIACGSAA
SGESFENVER IAKFAAENVF TIGCALDPAS VPGQGLPRVL ETSQIEFGMG IHNEPGFKTT
ELKSGHEMVS DMISHVFNSK LLKASSQKLN SKKVVLLVNN LGAISNLELG LVSNEACNEI
KKHGFEIVRA FQGTFMTGLA MPGASISVLV VPSSSADEQE ILKFIDLPAH APGWNNLIPV
ADKSSKSDAI VDNERRANLA SQTSNKTHER SEMWVKISNS VYDSSVVHEQ EITYLDSVMG
DGDCGQVLLS GTTSVKNAAN SSKIPSNNIA AAVSTISGLL EDSMGGTSGI IYCLFFDGVS
QHLSKAGYSS DNGAMPSAEV WGEALSNGLE TIQRYSTAKV GDRTLIDALH PFIETFKASG
GDLAQSLESA KQGAKKTEEM VPLRGRAVYT GKGKGHADAG AVGVCAVIEG ILNALH
//
