DAK1_SCHPO
ID DAK1_SCHPO Reviewed; 580 AA.
AC O13902;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Dihydroxyacetone kinase 1;
DE Short=DHA kinase 1;
DE EC=2.7.1.28;
DE EC=2.7.1.29 {ECO:0000269|PubMed:10091325};
DE AltName: Full=Glycerone kinase 1;
DE AltName: Full=Triokinase 1;
DE AltName: Full=Triose kinase 1;
GN Name=dak1; ORFNames=SPAC22A12.11;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC STRAIN=IFO 0354;
RX PubMed=10091325; DOI=10.1007/s002530051381;
RA Itoh N., Tujibata Y., Liu J.Q.;
RT "Cloning and overexpression in Escherichia coli of the gene encoding
RT dihydroxyacetone kinase isoenzyme I from Schizosaccharomyces pombe, and its
RT application to dihydroxyacetone phosphate production.";
RL Appl. Microbiol. Biotechnol. 51:193-200(1999).
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).
CC -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of
CC glyceraldehyde. {ECO:0000250, ECO:0000269|PubMed:10091325}.
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:0000269|PubMed:10091325};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.01 mM for dihydroxyacetone {ECO:0000269|PubMed:10091325};
CC KM=0.63 mM for ATP {ECO:0000269|PubMed:10091325};
CC Vmax=29.4 mmol/min/mg enzyme {ECO:0000269|PubMed:10091325};
CC -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC from glycerol (oxidative route): step 2/2.
CC {ECO:0000305|PubMed:10091325}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10091325}.
CC -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC {ECO:0000305}.
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DR EMBL; AB010078; BAA24186.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16581.1; -; Genomic_DNA.
DR PIR; T43310; T43310.
DR RefSeq; NP_593241.1; NM_001018638.2.
DR AlphaFoldDB; O13902; -.
DR SMR; O13902; -.
DR BioGRID; 278300; 14.
DR STRING; 4896.SPAC22A12.11.1; -.
DR iPTMnet; O13902; -.
DR MaxQB; O13902; -.
DR PaxDb; O13902; -.
DR PRIDE; O13902; -.
DR EnsemblFungi; SPAC22A12.11.1; SPAC22A12.11.1:pep; SPAC22A12.11.
DR GeneID; 2541809; -.
DR KEGG; spo:SPAC22A12.11; -.
DR PomBase; SPAC22A12.11; dak1.
DR VEuPathDB; FungiDB:SPAC22A12.11; -.
DR eggNOG; KOG2426; Eukaryota.
DR HOGENOM; CLU_017054_6_0_1; -.
DR InParanoid; O13902; -.
DR OMA; TALNMNG; -.
DR PhylomeDB; O13902; -.
DR BRENDA; 2.7.1.29; 5613.
DR UniPathway; UPA00617; UER00669.
DR PRO; PR:O13902; -.
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; IDA:PomBase.
DR GO; GO:0050354; F:triokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IDA:PomBase.
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 1: Evidence at protein level;
KW ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..580
FT /note="Dihydroxyacetone kinase 1"
FT /id="PRO_0000121520"
FT DOMAIN 8..349
FT /note="DhaK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT DOMAIN 384..580
FT /note="DhaL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT ACT_SITE 221
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT BINDING 53..56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
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 458..459
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 512..513
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 565..567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 580 AA; 62316 MW; 8AC984318610E08D CRC64;
MDKHFINDPE VLVLDGLKSL ADMNKTLTVH EEGKFIYFHD YNKKNVSVIS GGGAGHEPTH
SSFVGKGMLT AAVSGSIFAS PSSKQIYTGI KQVESEAGTL VICKNYTGDI LHFGMALEKQ
RTAGKKAELI AVADDVSVGR KKSGKVGRRG LSGTVLVHKI AGAAAARGLP LEAVTTIAKA
AIDNLVSIGA SLAHVHVPGH EPIAKEDEMK HDEMELGMGI HNEPGCKRIS PIPSIDDLIA
QMLKQMLDQS DKDRAYVKIE GDDEVVLLMN NLGGLSMLEF SAISHKVKEA LAKEYKINPV
RIFAGPFTTS LNGLGFGITL LRTTDRVKVE GEEYSLVDLI DQPVEAIGWP LCQPSDLKSK
NKIGNVSIEE GQKDVKSPVT VDKEKVRQAI VNSMENLIKA EPKITKFDTM AGDGDCGTTL
KRGAEGVLKF VKSDKFSDDP IRIVRDIADV IEDNMDGTSG ALYAIFFHGF AKGMKDTLEK
SKDISSKTWA AGLKVALDTL FKYTPARPGD STMCDALVPF VETFVKTNDL NAAVEEARKG
ADATADMQAK LGRAVYVGDD VKVPDAGALG VVAIVEGFTK
