ID A0A1B9GKG3_9TREE Unreviewed; 582 AA.
AC A0A1B9GKG3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Dihydroxyacetone kinase {ECO:0000313|EMBL:OCF31435.1};
GN ORFNames=I316_06837 {ECO:0000313|EMBL:OCF31435.1};
OS Kwoniella heveanensis BCC8398.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296120 {ECO:0000313|EMBL:OCF31435.1, ECO:0000313|Proteomes:UP000092666};
RN [1] {ECO:0000313|EMBL:OCF31435.1, ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|EMBL:OCF31435.1,
RC ECO:0000313|Proteomes:UP000092666};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus heveanensis BCC8398.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC8398 {ECO:0000313|Proteomes:UP000092666};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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}.
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DR EMBL; KV700134; OCF31435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B9GKG3; -.
DR STRING; 1296120.A0A1B9GKG3; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000092666; 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, ECO:0000313|EMBL:OCF31435.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000092666};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..341
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 374..573
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT REGION 338..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 216
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 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 582 AA; 60236 MW; 2DC299A4201CA276 CRC64;
MASKHLHDDP AALPLQYLHG LAVLNPDLSV DESHKVLHKR NHDRNTVAVI SGGGSGHEVD
AGFVGQGMLS AAVAGNVFAS PNARQIRRAL TLVDNEKGTL VVVKRYTGDV LQFGLAGESV
PGNVEFLVVG DDVAVGRKQG AIVGRRGLAG VTLVYKVAGY LAQQGLALDE IRRVASLVAS
NVGTIGSSLA HCHVPGTETE ESTLQSDELE IGTGIHNEPG LLKLRPVPSA SELVERMVAL
LTATDDPDRS FLSFKGDGKD SIVLMINNLG GISELELVAL VTPILAAFAR RGISVARLLT
GTFMSSLDMS GFSITACLLP RDVDSDVILQ ALDGSTDAPG WRKSSVPLPK PTITPPAAGL
APSPPSGLSA PVPQDFIAAI RSACHRVIAA EPEITRYDVI AGDGDCGLTL TSGAEGVLKA
IEDGSIDGGD ITNSIKRIGA VIEDRMGGTS GALYAIFFAG LAQELSSQTG QTSPAIWSNA
LSAAFNKLCQ YTSARPPSRT LVDPLAAFTE VLAANPHQLA EAAKSAKDAA LNTAKLVASA
GRAAYVDQAA LQEEDVPDPG AWGLTILFEG IHASVAGSGG AQ
//
