ID A0A165JUC8_XYLHT Unreviewed; 472 AA.
AC A0A165JUC8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 18-JUN-2025, entry version 25.
DE SubName: Full=DAK1/DegV-like protein {ECO:0000313|EMBL:KZF26640.1};
GN ORFNames=L228DRAFT_243134 {ECO:0000313|EMBL:KZF26640.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF26640.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF26640.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF26640.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
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; KV407454; KZF26640.1; -; Genomic_DNA.
DR RefSeq; XP_018192195.1; XM_018331614.1.
DR AlphaFoldDB; A0A165JUC8; -.
DR FunCoup; A0A165JUC8; 528.
DR STRING; 1328760.A0A165JUC8; -.
DR GeneID; 28896751; -.
DR InParanoid; A0A165JUC8; -.
DR OMA; QCDIENK; -.
DR OrthoDB; 1724672at2759; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000076632; 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; 1.25.40.340:FF:000001; Dihydroxyacetone kinase 1; 1.
DR FunFam; 3.30.1180.20:FF:000001; Dihydroxyacetone kinase 1; 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: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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076632};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..233
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 269..468
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
SQ SEQUENCE 472 AA; 49826 MW; 1303CD4B35FFEE8F CRC64;
MAVEKAKARG LDVEMVVVGD DVGVGRKKGG KVGRRGIAGT ALVQKIAGAL AATGAPLKDV
YGVAKLSSEN LVSVGASLSH VHVPGRTLED PNAGEALSIE EVEIGMGIHN EPGYAKVKMA
LPELVTTMLK QLLDQSDKDR AFLKIAPEDE VVLLINNLGG VSPLELGGIT AEVATQLDKD
YEIKPVRVLS GTFMTSLNGL GFSITILKLV DTGLGQGRSM LELLDAPAEA TGWQAAVSPE
TWSEKFRHNS VALDEEPPTE PTNLRVDRTY LQEVLASGLN RLIEAEPDIT TYDTIAGDGD
CGIGLRRGAE SILKYLEKYK GTDDIVVALT DITRIVETSM DGTSGALYAI FLNALANGLR
LQSPSSPSEV TPAIWGKGLK YSLNSLAKYT PARPGDRTLV DALDPFVETL IASDDPKKAA
DAARKGAENT KGMVASLGRT VYVGGEGWQG VPDPGAHGLS QFLTGLVEGL SR
//
