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Database: UniProt
Entry: A0A6A6QKH4_9PEZI
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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}.
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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
//
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