ID A0A9P6LNY7_9PEZI Unreviewed; 574 AA.
AC A0A9P6LNY7;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE SubName: Full=Dihydroxyacetone kinase {ECO:0000313|EMBL:KAF9880468.1};
GN ORFNames=CkaCkLH20_02422 {ECO:0000313|EMBL:KAF9880468.1};
OS Colletotrichum karsti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum boninense species complex.
OX NCBI_TaxID=1095194 {ECO:0000313|EMBL:KAF9880468.1, ECO:0000313|Proteomes:UP000781932};
RN [1] {ECO:0000313|EMBL:KAF9880468.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CkLH20 {ECO:0000313|EMBL:KAF9880468.1};
RA He L.;
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF9880468.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CkLH20 {ECO:0000313|EMBL:KAF9880468.1};
RA Li H.;
RT "Whole genome sequencing of Colletotrichum sp.";
RL Submitted (NOV-2020) 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:KAF9880468.1}.
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DR EMBL; JAATWM020000005; KAF9880468.1; -; Genomic_DNA.
DR RefSeq; XP_038749929.1; XM_038885141.1.
DR AlphaFoldDB; A0A9P6LNY7; -.
DR GeneID; 62158215; -.
DR OrthoDB; 1724672at2759; -.
DR Proteomes; UP000781932; 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; 1.25.40.340:FF:000001; Dihydroxyacetone kinase 1; 1.
DR FunFam; 3.30.1180.20:FF:000001; Dihydroxyacetone kinase 1; 1.
DR FunFam; 3.40.50.10440:FF:000001; Dihydroxyacetone kinase, DhaK subunit; 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, ECO:0000313|EMBL:KAF9880468.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000781932};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..337
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 375..571
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT ACT_SITE 219
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 53..56
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 574 AA; 59826 MW; 3969EC5325D72F75 CRC64;
MSQHFYDEAE NLVLDALESL ALTHSGLSFD KSKKVIWLTN NDSKKVSILS GGGAGHEPAH
AGFVGDSMLT AAVSGSIFAS PSVAQIVSGI SRVASPAGVL LVVKNYTGDV FHFHLAAEKA
KASLGIPVEV IVVGDDVSVG RKKSGKVGRR GLAGTVLVHK ILGAYKETGA SLADVLKLGK
TVGDNLVTVG ASLEHVHIPG REAAAPSAGD QVELGMGIHN EPGCQVLKPR PELPKLIEQM
LTQLLDTKDA DRAYVDFSDA KDVVLLVNNL GGVSPLEFSG ITAKVVNALG GRGLKLARVI
SGTYMTSLNG PGFSITLLKA TPEILKYVDA STDALGWAYT PRNETGSDAK QRIVESGETS
HGSDGSKSGV QLNVETFKKV VAEAHKRIAD AEPQITDHDT KVGDGDCGVT LLRGAKAVSK
YAESSSVSDD AVRTAIDLTN VIEDNMDGTS GAIYSIFFAA LSSELRKASA GVLDLKAWTK
VAVGALEKLQ QATPARQGDR TLLDALEPFV KTLEKTGSVK DAVAEARKGV EATKGMAASL
GRAVYVEESA WGKVPDPGAE GVLAILEGLE AATS
//
