DAK2_SCHPO
ID DAK2_SCHPO Reviewed; 591 AA.
AC O74215; Q9P7U0; Q9URP4; Q9UU48;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Dihydroxyacetone kinase 2;
DE Short=DHA kinase 2;
DE EC=2.7.1.28;
DE EC=2.7.1.29;
DE AltName: Full=Glycerone kinase 2;
DE AltName: Full=Triokinase 2;
DE AltName: Full=Triose kinase 2;
GN Name=dak2; Synonyms=dak1; ORFNames=SPAC977.16c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IFO 0354;
RX PubMed=9804990; DOI=10.1016/s0167-4781(98)00152-3;
RA Kimura T., Takahashi M., Yoshihara K., Furuichi T., Suzuki K., Imai K.,
RA Karita S., Sakka K., Ohmiya K.;
RT "Cloning and characterization of two genes encoding dihydroxyacetone kinase
RT from Schizosaccharomyces pombe IFO 0354.";
RL Biochim. Biophys. Acta 1442:361-368(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 103-168.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
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 -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC from glycerol (oxidative route): step 2/2.
CC -!- MISCELLANEOUS: Seems to be missing in strain 972.
CC -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC {ECO:0000305}.
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DR EMBL; AF059204; AAC78808.1; -; Genomic_DNA.
DR EMBL; AF059205; AAC83220.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB69638.1; -; Genomic_DNA.
DR EMBL; AB027813; BAA87117.1; -; Genomic_DNA.
DR PIR; T43702; T43702.
DR PIR; T43721; T43721.
DR PIR; T50287; T50287.
DR RefSeq; NP_592787.1; NM_001018187.2.
DR AlphaFoldDB; O74215; -.
DR SMR; O74215; -.
DR BioGRID; 278301; 1.
DR STRING; 4896.SPAC977.16c.1; -.
DR iPTMnet; O74215; -.
DR MaxQB; O74215; -.
DR PaxDb; O74215; -.
DR EnsemblFungi; SPAC977.16c.1; SPAC977.16c.1:pep; SPAC977.16c.
DR GeneID; 2541810; -.
DR KEGG; spo:SPAC977.16c; -.
DR PomBase; SPAC977.16c; dak2.
DR VEuPathDB; FungiDB:SPAC977.16c; -.
DR eggNOG; KOG2426; Eukaryota.
DR HOGENOM; CLU_017054_6_0_1; -.
DR InParanoid; O74215; -.
DR OMA; EPKITHY; -.
DR PhylomeDB; O74215; -.
DR BioCyc; MetaCyc:MON-16996; -.
DR Reactome; R-SPO-70350; Fructose catabolism.
DR UniPathway; UPA00617; UER00669.
DR PRO; PR:O74215; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; ISO:PomBase.
DR GO; GO:0050354; F:triokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; IMP:PomBase.
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 Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF101473; SSF101473; 1.
DR TIGRFAMs; TIGR02361; dak_ATP; 1.
DR PROSITE; PS51481; DHAK; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..591
FT /note="Dihydroxyacetone kinase 2"
FT /id="PRO_0000121521"
FT DOMAIN 8..344
FT /note="DhaK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT DOMAIN 384..587
FT /note="DhaL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT ACT_SITE 223
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT BINDING 58..61
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 413..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 459..460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 511..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 572..574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 9
FT /note="D -> E (in Ref. 1; AAC78808)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="I -> V (in Ref. 1; AAC83220)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="L -> P (in Ref. 1; AAC78808)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="T -> I (in Ref. 1; AAC78808/AAC83220)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="H -> R (in Ref. 1; AAC78808/AAC83220)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="N -> K (in Ref. 1; AAC78808/AAC83220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 62127 MW; 7FCCEB2EB5CC1C21 CRC64;
MSVKQFVSDG HIVRPYLLGL ARSNPGLTVI EHDRVIYRTA SAPGSGDLPK VTLVSGGGSG
HEPTHAGFVG DGALDAVACG DIFASPSTKQ IYSALKAVAS PKGTLIIVKN YTGDIIHFGL
AAERAKAAGM NVELVAVGDD VSVGKKRGAL VGRRGLGATV LVHKIAGSAA ALGLDLHQVA
QVAQSVIDNA ATIAASLDHC AVPGRKFETN LGPDEYEIGM GIHNEPGTFK SSPLPSIPEL
VTEMLSILFG EKNPDNSFVE FSSKDDVILL VNNMGGMSNL ELGYATEVVS EQLAKRGIIP
KRTMSGTFVT ALNGPGFGIT LVNASKATPD IFKYFDLPTT ASGWNVSYHN AKDWEVLADG
KVPTAPALEH TRNEKHSGVK ADPKMFTKIL KAAVDAINEF EPKTTWYDTI AGDGDCGTTL
VNGGEAITKA INDKSIRLDD GVNGIDDLAY IVEDSMGGTS GGLYSIYLSA LAKGVHESGD
SELSVHTFAF ASKYALDALF KYTRARKGFR TLIDAIQPFV ETLNEGKGLD AAAKAATEGS
EQTRKMDAVV GRASYVAKEE LHKLDSEGGL PDPGAFALAA ILNAIVEASE H
