DHAK_DICDI
ID DHAK_DICDI Reviewed; 648 AA.
AC Q55EE0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Probable dihydroxyacetone kinase;
DE Short=DHA kinase;
DE EC=2.7.1.28;
DE EC=2.7.1.29;
DE AltName: Full=Glycerone kinase;
DE AltName: Full=Triokinase;
DE AltName: Full=Triose kinase;
GN Name=dhak; Synonyms=dak; ORFNames=DDB_G0269274;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of
CC glyceraldehyde. {ECO:0000250}.
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;
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;
CC -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL71987.1; -; Genomic_DNA.
DR RefSeq; XP_645841.1; XM_640749.1.
DR AlphaFoldDB; Q55EE0; -.
DR SMR; Q55EE0; -.
DR STRING; 44689.DDB0266459; -.
DR PaxDb; Q55EE0; -.
DR PRIDE; Q55EE0; -.
DR EnsemblProtists; EAL71987; EAL71987; DDB_G0269274.
DR GeneID; 8616785; -.
DR KEGG; ddi:DDB_G0269274; -.
DR dictyBase; DDB_G0269274; dhak.
DR eggNOG; KOG2426; Eukaryota.
DR HOGENOM; CLU_017054_6_1_1; -.
DR InParanoid; Q55EE0; -.
DR OMA; TALNMNG; -.
DR PhylomeDB; Q55EE0; -.
DR Reactome; R-DDI-70350; Fructose catabolism.
DR PRO; PR:Q55EE0; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0050354; F:triokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.340; -; 1.
DR InterPro; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR Pfam; PF02733; Dak1; 2.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF101473; SSF101473; 1.
DR PROSITE; PS51481; DHAK; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Lyase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..648
FT /note="Probable dihydroxyacetone kinase"
FT /id="PRO_0000328437"
FT DOMAIN 7..391
FT /note="DhaK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT DOMAIN 433..645
FT /note="DhaL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT ACT_SITE 247
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT BINDING 55..58
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 462..465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 506..507
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 562..563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 630..632
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 648 AA; 71006 MW; F841383A0B1EEE92 CRC64;
MKKIINNPQN VVSEMIDGFT QSSRDLLKLK GNFNVVVRSD YSQIKDRVTL ISGGGSGHEP
AHIGYIGNAM LTGAVCGDVF ASPSAKQIFM AIKSVAGKMG CILIVKNYMG DNGSFSIARE
MCKSQLPDIR VEIITVDDDI SSILMKLNEF SNDNNDNIQD IRDKYKSITN RRGIAGTVLV
HKILGGLAEQ GKSIDEILKF YNKYISPSKS LNLVTMGVGL SSCIIPSVGS PSFTLNEKEM
EIGLGIHGEF GIEKVELKPS KQIIKSLIDN LLKILPYSNN NNNNNNNNNN NNNNNNNNNN
NSCGISCGSD GEDKSLIVLI NNLGSTTNME MAIATNDCLN YLHEKGFTVE RLITGTLMTS
LEMAGISISL LLIKNNQIIN LIDLKTNAMG WPNSVLKPYK NKEDSILTLD ENDSHEIKYD
NLKSITISKE NGEILKEIVL LGCNSLIENS NKLTDLDKQV GDGDLGTTLE NLSKSIKKSI
DTIPFDKPCY TFRKISLIIQ ELIGGSSGLF YSIFFLRLSN SLYERSTVNG KNQISTNDWG
LSLIDAVNAI KELGKADIGD CTMLDSLIPA INKINQCCKD NENSSSSFDL LNTLKLASKE
AQLGSESTIE MIAKKGRSSY LGERTSHIMD PGAHAIEIIF KSFLSIKK
