ID U9T842_RHIID Unreviewed; 610 AA.
AC U9T842;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Dihydroxyacetone kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GLOINDRAFT_336308 {ECO:0000313|EMBL:ESA04330.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:ESA04330.1};
RN [1] {ECO:0000313|EMBL:ESA04330.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM 197198 {ECO:0000313|EMBL:ESA04330.1};
RG DOE Joint Genome Institute;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei-dit-Frey N., Gianinazzi-Pearson V.,
RA Gilbert B., Handa Y., Hijri M., Kaul R., Kawaguchi M., Krajinski F.,
RA Lammers P., Lapierre D., Masclaux F.G., Murat C., Morin E., Ndikumana S.,
RA Pagni M., Petitpierre D., Requena N., Rosikiewicz P., Riley R., Saito K.,
RA San Clemente H., Shapiro H., van Tuinen D., Becard G., Bonfante P.,
RA Paszkowski U., Shachar-Hill Y., Young J.P., Sanders I.R., Henrissat B.,
RA Rensing S.A., Grigoriev I.V., Corradi N., Roux C., Martin F.;
RT "The genome of an arbuscular mycorrhizal fungus provides insights into the
RT evolution of the oldest plant symbiosis.";
RL Submitted (JUL-2013) 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; KI294387; ESA04330.1; -; Genomic_DNA.
DR AlphaFoldDB; U9T842; -.
DR eggNOG; KOG2426; Eukaryota.
DR HOGENOM; CLU_017054_6_0_1; -.
DR UniPathway; UPA00617; UER00669.
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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..351
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 387..606
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 66..69
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 610 AA; 66238 MW; FC453EF17DFB4CE5 CRC64;
MESNKESPSR RPKHFVNDPN KIVIESLRGL CLSYPSLRFI EKEKIVYRAD IDDIRKKQVT
LISGGGAGHE PAHVAFVGPN LLSAAVSGNI FASPSTSQIL AAIRRVQSPH GTLLIVKNYT
GDCLNFGLAA EKAKAEGIKV EIVIVGDDVG VGRQQSGLVG RRGLAGTIFV HKIAGAMAAK
RASLKEVKNA ALLVAENIGT IGVTFDRCTI PGTTKSSFLP DDEIELGMGI HGEPGFQKIS
LPPSSELVQK MLDTIINTND EDRSFLDINP EKDKIALLVN NLGGISALEL GVVLNDAFNY
LVKKNFYVRR VYVGHYMTSL NMPGVSLSIL KLPKNLDVVP LLDIKAETPG WVNHSKVDIS
NLDVSLDEKV SFKEKEEDLF VVNVNSQLFE STIKAACNAL IQAEPEITKY DTIVGDGDCG
LTLKYGATDI LKALEEKQIM TNDLSGGLMK ISNILERGGT IGFLYCLFIG AISNSLRYFV
AAKIEDNDNK KDQILVDGKC IGASLKSALS TLQNYTPARK GDRTMMDVII PFITSFTDIL
FSTNDDNTMI AFKDAIEAAR IGAESTKGMK PKLGRSTYIA NNIIKEAQVP DPGAWAAYVI
LNGIYDHLSE
//
