ID A0A446BFY4_9PEZI Unreviewed; 528 AA.
AC A0A446BFY4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=87ec389b-72fe-4f1f-bfb6-35a73704d50d {ECO:0000313|EMBL:SPQ21343.1};
GN ORFNames=TT172_LOCUS3762 {ECO:0000313|EMBL:SPQ21343.1};
OS Thermothielavioides terrestris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ21343.1, ECO:0000313|Proteomes:UP000289323};
RN [1] {ECO:0000313|EMBL:SPQ21343.1, ECO:0000313|Proteomes:UP000289323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Huttner S., Dainat J.;
RL Submitted (APR-2018) 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; OUUZ01000008; SPQ21343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A446BFY4; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000289323; 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:SF1; YALI0E20691P; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..349
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 326..521
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
SQ SEQUENCE 528 AA; 56072 MW; 9C148AF2BCA0D835 CRC64;
MSSKHYFPSS SATSLVPRYL SALVREHPQL ELIPSQRVVY NPSHDRSCVA VISGGGSEHE
PSWSGFVGDG LLAAAVCGDI FASPSTKQVL AAVDAVPSDA GVILMITNYT GDKLHFGLAA
ERAKAAGTCG GGRIAVLPST DDVSIGRSRT KAVGRRGMPG HVITLKIVGA AAASKRSFDE
CVAIGLAVND QLVSIGSSLD HCHVPGRENH ESLGDDACAI GAGIHNEPAQ QEISPFPSVE
DVVDRCLRLL CDPADTERAF VDFSNVDDSI VLLVNNYGGL SNLELGALTD EVLRQLEANW
RIRPVTNGDL PKPHISEEED IRVDARSLDA LIRGGCTAAI AAEPDLTRWD MVMGDGDCGE
AVKRVCEALV SILDKGAARG GSLLKLLFAA SDAVDDMGGT LGAILGILLS AFITELRLRA
GAGRVNQETV AKALQAAVEV LKKHTAAREG DRTVMDVLLP FAEAFSQSFD FQRAVNVAME
KAEATRYLKP KFGRATYVGK EEELPDPGAW ALAVFLRGMW TALQAHQE
//
