ID A0A316UJG4_9BASI Unreviewed; 616 AA.
AC A0A316UJG4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Putative DAK2-dihydroxyacetone kinase {ECO:0000313|EMBL:PWN25422.1};
GN ORFNames=BDZ90DRAFT_255682 {ECO:0000313|EMBL:PWN25422.1};
OS Jaminaea rosea.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Jaminaea.
OX NCBI_TaxID=1569628 {ECO:0000313|EMBL:PWN25422.1, ECO:0000313|Proteomes:UP000245884};
RN [1] {ECO:0000313|EMBL:PWN25422.1, ECO:0000313|Proteomes:UP000245884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 5214 {ECO:0000313|EMBL:PWN25422.1,
RC ECO:0000313|Proteomes:UP000245884};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819676; PWN25422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316UJG4; -.
DR STRING; 1569628.A0A316UJG4; -.
DR OrthoDB; 6043at2759; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000245884; 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:SF14; CHROMOSOME 1, WHOLE GENOME SHOTGUN SEQUENCE; 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:PWN25422.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000245884};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..357
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 412..611
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT ACT_SITE 231
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 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 616 AA; 64953 MW; 34B795A8AC6CA37B CRC64;
MSTKHIFDNP EGLVDKTLRG AIAVNPALRL YKPHKVIYDS THSNSKVAIM AGGGAGHEPG
QAGLIGKGML AAAISGDVFA SPSAAQICTG IDLANTDKGV IFIINNYTGD QLHFGLAAEK
ARSALAISGN KTSGGVECVT VADDVAVGRA KGGLVGRRGL GMNPFSCKVL GAAAERGLSV
KEIKKLGDTL IDNSVTIGTS LDHCHVPGRS KDPKEWGALP QEACEIGMGI HNEPGFKRLD
KTPPPDKLIA EMLDYMLNQN DKDRAYLPFS AGDAPVLFIN NLGGISQLEL FAALDETIAQ
LGKTYDLHPA RVYCNAYMTS LNAPGFGITL VKHREVTKAC GVDLLDLLDD PTDAYAWTGV
TRGWPSNPRD REAEEKEAEQ RLAEVQKKGG AVSMLEADAK EKADGPSNAD PEQTKKAIWS
MCQAAIDAEP SITRHDTIVG DGDCGTGLAT FAKAIQQGLD SGNVDLKVAA STVMSIGTIA
SDVYGGTSGA IYELFLAGLA QAFTSMPRQP ATIKEWSSAS SQALKSLFTF TPARPGMRTL
IDALEPFVVE LEKSQDLSKA VAAAKEGMEK TKRLDAKLGR SVYQGEGNEE MKQTPDPGAE
GIAEVVAGLL KGLGGK
//
