Full text data of DAK
DAK
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing); ATP-dependent dihydroxyacetone kinase; DHA kinase; 2.7.1.28; 2.7.1.29 (Glycerone kinase; Triokinase; Triose kinase; FAD-AMP lyase (cyclizing); 4.6.1.15; FAD-AMP lyase (cyclic FMN forming); FMN cyclase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing); ATP-dependent dihydroxyacetone kinase; DHA kinase; 2.7.1.28; 2.7.1.29 (Glycerone kinase; Triokinase; Triose kinase; FAD-AMP lyase (cyclizing); 4.6.1.15; FAD-AMP lyase (cyclic FMN forming); FMN cyclase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00551024
IPI00551024 THYRO1000951 protein glycerol metabolism soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00551024 THYRO1000951 protein glycerol metabolism soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q3LXA3
ID DHAK_HUMAN Reviewed; 575 AA.
AC Q3LXA3; Q53EQ9; Q9BVA7; Q9H895;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-NOV-2010, sequence version 2.
DT 22-JAN-2014, entry version 83.
DE RecName: Full=Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing);
DE Includes:
DE RecName: Full=ATP-dependent 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;
DE Includes:
DE RecName: Full=FAD-AMP lyase (cyclizing);
DE EC=4.6.1.15;
DE AltName: Full=FAD-AMP lyase (cyclic FMN forming);
DE AltName: Full=FMN cyclase;
GN Name=DAK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FAD-AMP LYASE ACTIVITY, AND
RP VARIANT THR-185.
RC TISSUE=Brain;
RX PubMed=16289032; DOI=10.1016/j.bbrc.2005.10.142;
RA Cabezas A., Costas M.J., Pinto R.M., Couto A., Cameselle J.C.;
RT "Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as
RT ATP-dependent dihydroxyacetone kinases.";
RL Biochem. Biophys. Res. Commun. 338:1682-1689(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-185.
RC TISSUE=Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-185.
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CATALYTIC ACTIVITY, FUNCTION, IDENTITY OF TRIOKINASE AND
RP DIHYDROXYACETONE KINASE, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=4688871;
RA Beutler E., Guinto E.;
RT "Dihydroxyacetone metabolism by human erythrocytes: demonstration of
RT triokinase activity and its characterization.";
RL Blood 41:559-568(1973).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone
CC and of glyceraldehyde, and the splitting of ribonucleoside
CC diphosphate-X compounds among which FAD is the best substrate.
CC -!- CATALYTIC ACTIVITY: ATP + glycerone = ADP + glycerone phosphate.
CC -!- CATALYTIC ACTIVITY: ATP + D-glyceraldehyde = ADP + D-
CC glyceraldehyde 3-phosphate.
CC -!- CATALYTIC ACTIVITY: FAD = AMP + riboflavin cyclic-4',5'-phosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- COFACTOR: Manganese or cobalt; for FAD-AMP lyase activity (By
CC similarity).
CC -!- ENZYME REGULATION: Each activity is inhibited by the substrate(s)
CC of the other.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for dihydroxyacetone;
CC KM=11 uM for glyceraldehyde;
CC pH dependence:
CC Optimum pH is 6.6;
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level).
CC -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC -!- SIMILARITY: Contains 1 DhaK domain.
CC -!- SIMILARITY: Contains 1 DhaL domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; DQ138290; ABA10576.1; -; mRNA.
DR EMBL; AK023915; BAB14722.1; -; mRNA.
DR EMBL; AK223580; BAD97300.1; -; mRNA.
DR EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001341; AAH01341.1; -; mRNA.
DR RefSeq; NP_056348.2; NM_015533.3.
DR UniGene; Hs.6278; -.
DR ProteinModelPortal; Q3LXA3; -.
DR SMR; Q3LXA3; 3-553.
DR MINT; MINT-5001370; -.
DR STRING; 9606.ENSP00000310493; -.
DR PhosphoSite; Q3LXA3; -.
DR DMDM; 311033370; -.
DR REPRODUCTION-2DPAGE; IPI00551024; -.
DR PaxDb; Q3LXA3; -.
DR PRIDE; Q3LXA3; -.
DR DNASU; 26007; -.
DR Ensembl; ENST00000394900; ENSP00000378360; ENSG00000149476.
DR GeneID; 26007; -.
DR KEGG; hsa:26007; -.
DR UCSC; uc001nre.3; human.
DR CTD; 26007; -.
DR GeneCards; GC11P061100; -.
DR HGNC; HGNC:24552; DAK.
DR HPA; HPA039486; -.
DR neXtProt; NX_Q3LXA3; -.
DR PharmGKB; PA142672014; -.
DR eggNOG; COG2376; -.
DR HOGENOM; HOG000234158; -.
DR HOVERGEN; HBG079502; -.
DR InParanoid; Q3LXA3; -.
DR KO; K00863; -.
DR OMA; LNMNGFS; -.
DR OrthoDB; EOG71K630; -.
DR PhylomeDB; Q3LXA3; -.
DR BRENDA; 2.7.1.29; 2681.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; DAK; human.
DR GeneWiki; DAK_(gene); -.
DR GenomeRNAi; 26007; -.
DR NextBio; 47741; -.
DR PMAP-CutDB; Q3LXA3; -.
DR PRO; PR:Q3LXA3; -.
DR ArrayExpress; Q3LXA3; -.
DR Bgee; Q3LXA3; -.
DR CleanEx; HS_DAK; -.
DR Genevestigator; Q3LXA3; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034012; F:FAD-AMP lyase (cyclizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050354; F:triokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR InterPro; IPR004006; Dak1.
DR InterPro; IPR012734; DhaK_ATP.
DR InterPro; IPR004007; DhaL_dom.
DR Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; 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; Cobalt; Complete proteome; FAD; Flavoprotein; Kinase;
KW Lyase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Polymorphism; Reference proteome; Transferase.
FT CHAIN 1 575 Bifunctional ATP-dependent
FT dihydroxyacetone kinase/FAD-AMP lyase
FT (cyclizing).
FT /FTId=PRO_0000121525.
FT DOMAIN 9 336 DhaK.
FT DOMAIN 372 571 DhaL.
FT NP_BIND 401 404 ATP (By similarity).
FT NP_BIND 446 447 ATP (By similarity).
FT NP_BIND 494 495 ATP (By similarity).
FT NP_BIND 556 558 ATP (By similarity).
FT REGION 56 59 Dihydroxyacetone binding (By similarity).
FT ACT_SITE 221 221 Tele-hemiaminal-histidine intermediate
FT (By similarity).
FT BINDING 109 109 Dihydroxyacetone (By similarity).
FT BINDING 114 114 Dihydroxyacetone (By similarity).
FT BINDING 486 486 ATP; via carbonyl oxygen (By similarity).
FT VARIANT 185 185 A -> T (in dbSNP:rs2260655).
FT /FTId=VAR_028108.
FT VARIANT 334 334 A -> G (in dbSNP:rs35723406).
FT /FTId=VAR_054780.
FT CONFLICT 7 7 V -> A (in Ref. 2; BAB14722).
FT CONFLICT 19 19 A -> S (in Ref. 3; BAD97300).
FT CONFLICT 75 75 V -> A (in Ref. 2; BAB14722).
FT CONFLICT 376 376 L -> P (in Ref. 2; BAB14722).
FT CONFLICT 497 497 D -> G (in Ref. 2; BAB14722).
SQ SEQUENCE 575 AA; 58947 MW; 4DB8C5326F65122C CRC64;
MTSKKLVNSV AGCADDALAG LVACNPNLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE
PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL
AREQARAEGI PVEMVVIGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEIAKQ
VNVVAKAMGT LGVSLSSCSV PGSKPTFELS ADEVELGLGI HGEAGVRRIK MATADEIVKL
MLDHMTNTTN ASHVPVQPGS SVVMMVNNLG GLSFLELGII ADATVRSLEG RGVKIARALV
GTFMSALEMP GISLTLLLVD EPLLKLIDAE TTAAAWPNVA AVSITGRKRS RVAPAEPQEA
PDSTAAGGSA SKRMALVLER VCSTLLGLEE HLNALDRAAG DGDCGTTHSR AARAIQEWLK
EGPPPASPAQ LLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKAKTSLPA WSAAMDAGLE
AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGADLLQVL TKAVKSAEAA AEATKNMEAG
AGRASYISSA RLEQPDPGAV AAAAILRAIL EVLQS
//
ID DHAK_HUMAN Reviewed; 575 AA.
AC Q3LXA3; Q53EQ9; Q9BVA7; Q9H895;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-NOV-2010, sequence version 2.
DT 22-JAN-2014, entry version 83.
DE RecName: Full=Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing);
DE Includes:
DE RecName: Full=ATP-dependent 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;
DE Includes:
DE RecName: Full=FAD-AMP lyase (cyclizing);
DE EC=4.6.1.15;
DE AltName: Full=FAD-AMP lyase (cyclic FMN forming);
DE AltName: Full=FMN cyclase;
GN Name=DAK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FAD-AMP LYASE ACTIVITY, AND
RP VARIANT THR-185.
RC TISSUE=Brain;
RX PubMed=16289032; DOI=10.1016/j.bbrc.2005.10.142;
RA Cabezas A., Costas M.J., Pinto R.M., Couto A., Cameselle J.C.;
RT "Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as
RT ATP-dependent dihydroxyacetone kinases.";
RL Biochem. Biophys. Res. Commun. 338:1682-1689(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-185.
RC TISSUE=Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-185.
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CATALYTIC ACTIVITY, FUNCTION, IDENTITY OF TRIOKINASE AND
RP DIHYDROXYACETONE KINASE, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=4688871;
RA Beutler E., Guinto E.;
RT "Dihydroxyacetone metabolism by human erythrocytes: demonstration of
RT triokinase activity and its characterization.";
RL Blood 41:559-568(1973).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone
CC and of glyceraldehyde, and the splitting of ribonucleoside
CC diphosphate-X compounds among which FAD is the best substrate.
CC -!- CATALYTIC ACTIVITY: ATP + glycerone = ADP + glycerone phosphate.
CC -!- CATALYTIC ACTIVITY: ATP + D-glyceraldehyde = ADP + D-
CC glyceraldehyde 3-phosphate.
CC -!- CATALYTIC ACTIVITY: FAD = AMP + riboflavin cyclic-4',5'-phosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- COFACTOR: Manganese or cobalt; for FAD-AMP lyase activity (By
CC similarity).
CC -!- ENZYME REGULATION: Each activity is inhibited by the substrate(s)
CC of the other.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for dihydroxyacetone;
CC KM=11 uM for glyceraldehyde;
CC pH dependence:
CC Optimum pH is 6.6;
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level).
CC -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC -!- SIMILARITY: Contains 1 DhaK domain.
CC -!- SIMILARITY: Contains 1 DhaL domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; DQ138290; ABA10576.1; -; mRNA.
DR EMBL; AK023915; BAB14722.1; -; mRNA.
DR EMBL; AK223580; BAD97300.1; -; mRNA.
DR EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001341; AAH01341.1; -; mRNA.
DR RefSeq; NP_056348.2; NM_015533.3.
DR UniGene; Hs.6278; -.
DR ProteinModelPortal; Q3LXA3; -.
DR SMR; Q3LXA3; 3-553.
DR MINT; MINT-5001370; -.
DR STRING; 9606.ENSP00000310493; -.
DR PhosphoSite; Q3LXA3; -.
DR DMDM; 311033370; -.
DR REPRODUCTION-2DPAGE; IPI00551024; -.
DR PaxDb; Q3LXA3; -.
DR PRIDE; Q3LXA3; -.
DR DNASU; 26007; -.
DR Ensembl; ENST00000394900; ENSP00000378360; ENSG00000149476.
DR GeneID; 26007; -.
DR KEGG; hsa:26007; -.
DR UCSC; uc001nre.3; human.
DR CTD; 26007; -.
DR GeneCards; GC11P061100; -.
DR HGNC; HGNC:24552; DAK.
DR HPA; HPA039486; -.
DR neXtProt; NX_Q3LXA3; -.
DR PharmGKB; PA142672014; -.
DR eggNOG; COG2376; -.
DR HOGENOM; HOG000234158; -.
DR HOVERGEN; HBG079502; -.
DR InParanoid; Q3LXA3; -.
DR KO; K00863; -.
DR OMA; LNMNGFS; -.
DR OrthoDB; EOG71K630; -.
DR PhylomeDB; Q3LXA3; -.
DR BRENDA; 2.7.1.29; 2681.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; DAK; human.
DR GeneWiki; DAK_(gene); -.
DR GenomeRNAi; 26007; -.
DR NextBio; 47741; -.
DR PMAP-CutDB; Q3LXA3; -.
DR PRO; PR:Q3LXA3; -.
DR ArrayExpress; Q3LXA3; -.
DR Bgee; Q3LXA3; -.
DR CleanEx; HS_DAK; -.
DR Genevestigator; Q3LXA3; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034012; F:FAD-AMP lyase (cyclizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050354; F:triokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR InterPro; IPR004006; Dak1.
DR InterPro; IPR012734; DhaK_ATP.
DR InterPro; IPR004007; DhaL_dom.
DR Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; 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; Cobalt; Complete proteome; FAD; Flavoprotein; Kinase;
KW Lyase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Polymorphism; Reference proteome; Transferase.
FT CHAIN 1 575 Bifunctional ATP-dependent
FT dihydroxyacetone kinase/FAD-AMP lyase
FT (cyclizing).
FT /FTId=PRO_0000121525.
FT DOMAIN 9 336 DhaK.
FT DOMAIN 372 571 DhaL.
FT NP_BIND 401 404 ATP (By similarity).
FT NP_BIND 446 447 ATP (By similarity).
FT NP_BIND 494 495 ATP (By similarity).
FT NP_BIND 556 558 ATP (By similarity).
FT REGION 56 59 Dihydroxyacetone binding (By similarity).
FT ACT_SITE 221 221 Tele-hemiaminal-histidine intermediate
FT (By similarity).
FT BINDING 109 109 Dihydroxyacetone (By similarity).
FT BINDING 114 114 Dihydroxyacetone (By similarity).
FT BINDING 486 486 ATP; via carbonyl oxygen (By similarity).
FT VARIANT 185 185 A -> T (in dbSNP:rs2260655).
FT /FTId=VAR_028108.
FT VARIANT 334 334 A -> G (in dbSNP:rs35723406).
FT /FTId=VAR_054780.
FT CONFLICT 7 7 V -> A (in Ref. 2; BAB14722).
FT CONFLICT 19 19 A -> S (in Ref. 3; BAD97300).
FT CONFLICT 75 75 V -> A (in Ref. 2; BAB14722).
FT CONFLICT 376 376 L -> P (in Ref. 2; BAB14722).
FT CONFLICT 497 497 D -> G (in Ref. 2; BAB14722).
SQ SEQUENCE 575 AA; 58947 MW; 4DB8C5326F65122C CRC64;
MTSKKLVNSV AGCADDALAG LVACNPNLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE
PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL
AREQARAEGI PVEMVVIGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEIAKQ
VNVVAKAMGT LGVSLSSCSV PGSKPTFELS ADEVELGLGI HGEAGVRRIK MATADEIVKL
MLDHMTNTTN ASHVPVQPGS SVVMMVNNLG GLSFLELGII ADATVRSLEG RGVKIARALV
GTFMSALEMP GISLTLLLVD EPLLKLIDAE TTAAAWPNVA AVSITGRKRS RVAPAEPQEA
PDSTAAGGSA SKRMALVLER VCSTLLGLEE HLNALDRAAG DGDCGTTHSR AARAIQEWLK
EGPPPASPAQ LLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKAKTSLPA WSAAMDAGLE
AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGADLLQVL TKAVKSAEAA AEATKNMEAG
AGRASYISSA RLEQPDPGAV AAAAILRAIL EVLQS
//