ID A0A6A6QKH4_9PEZI Unreviewed; 583 AA.
AC A0A6A6QKH4;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=Dak1-domain-containing protein {ECO:0000313|EMBL:KAF2492526.1};
GN ORFNames=BU16DRAFT_592157 {ECO:0000313|EMBL:KAF2492526.1};
OS Lophium mytilinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Mytilinidiales; Mytilinidiaceae; Lophium.
OX NCBI_TaxID=390894 {ECO:0000313|EMBL:KAF2492526.1, ECO:0000313|Proteomes:UP000799750};
RN [1] {ECO:0000313|EMBL:KAF2492526.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 269.34 {ECO:0000313|EMBL:KAF2492526.1};
RA Haridas S., Albert R., Binder M., Bloem J., Labutti K., Salamov A.,
RA Andreopoulos B., Baker S., Barry K., Bills G., Bluhm B., Cannon C.,
RA Castanera R., Culley D., Daum C., Ezra D., Gonzalez J., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B., Goodwin S., Spatafora J., Crous P.,
RA Grigoriev I.;
RT "101 Dothideomycetes genomes: a test case for predicting lifestyles and
RT emergence of pathogens.";
RL Stud. Mycol. 0:0-0(2020).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MU004193; KAF2492526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A6QKH4; -.
DR OrthoDB; 1724672at2759; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000799750; 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:0019588; P:anaerobic glycerol catabolic process; IEA:UniProtKB-UniPathway.
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; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR InterPro; IPR050861; Dihydroxyacetone_Kinase.
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:UP000799750};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..315
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 354..577
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT REGION 452..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 61154 MW; A72AA0C7A0AB840A CRC64;
MSLGKHFIND VTNPVERALR SMLLHDTALR LIESEKGGAG HEPAHAGFLG EGMLDICVSG
NTFASPSASQ VFAGVKSLPS PQGTLMIVKN YTGDKLNFGL AAEKAKAIGK RVNVVFVGDD
VAVEGNGLVG RRGLAGVAFV HKVAGALASS GADLDSTTAI AQKVADQMAT VGVSLDRCSV
PRRGEQEPLP FDQLEYGMGI HNEPGVRRAR IPSLSETVTR VLQMLTKKRS ISWTPTTTQC
LAVMVNNLGG LSVLELNVVT QEVVRQLRKD GLQIRRLLMG TFVSSLNGPG FSVTLLEVDP
QIEMLLDAPT TAPAWPKIIS PISISAADDQ IIHEADTEAV PVSEGTPLLP VSSALITTII
QSIVSSVFTS EPLITHYDTI AGDGDCGETL LNGANALLTE FSNPTSPTLS LPTVFHTIAT
VIERSMGGTS GAIYAIFLNA VSTALAKTST STDFRKTAPP SPPMSPSTGP QSQLSYSIII
ASAFRSGLTE LCKYTSARKG HRTLMDALIP FVDVFEESGD LIRAGNAARE GAEGTRSMKA
LLGRASYVGE SAFEGEKGGI PDPGALGVVS VVDGVCKGLA TES
//