ID   DHAK_HUMAN              Reviewed;         575 AA.
AC   Q3LXA3; Q53EQ9; Q9BVA7; Q9H895;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   07-JUL-2009, entry version 41.
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=2.7.1.29;
DE     AltName: Full=Glycerone 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, AND FAD-AMP LYASE ACTIVITY.
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].
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].
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 MRNA], AND VARIANT ALA-185.
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   [5]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone
CC       and the splitting of ribonucleoside diphosphate-X compounds among
CC       which FAD is the best substrate.
CC   -!- CATALYTIC ACTIVITY: ATP + glycerone = ADP + glycerone 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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC   -!- SIMILARITY: Contains 1 DAK1 (dihydroxyacetone kinase subunit 1)
CC       domain.
CC   -!- SIMILARITY: Contains 1 DAK2 (dihydroxyacetone kinase subunit 2)
CC       domain.
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DR   EMBL; DQ138290; ABA10576.1; -; mRNA.
DR   EMBL; AK023915; BAB14722.1; -; mRNA.
DR   EMBL; AK223580; BAD97300.1; -; mRNA.
DR   EMBL; BC001341; AAH01341.1; -; mRNA.
DR   IPI; IPI00551024; -.
DR   RefSeq; NP_056348.2; -.
DR   UniGene; Hs.6278; -.
DR   HSSP; P76015; 1OI2.
DR   PhosphoSite; Q3LXA3; -.
DR   REPRODUCTION-2DPAGE; IPI00551024; -.
DR   PRIDE; Q3LXA3; -.
DR   Ensembl; ENSG00000149476; Homo sapiens.
DR   GeneID; 26007; -.
DR   KEGG; hsa:26007; -.
DR   UCSC; uc001nre.1; human.
DR   GeneCards; GC11P060858; -.
DR   HGNC; HGNC:24552; DAK.
DR   PharmGKB; PA142672014; -.
DR   HOGENOM; Q3LXA3; -.
DR   HOVERGEN; Q3LXA3; -.
DR   BRENDA; 2.7.1.29; 247.
DR   BRENDA; 4.6.1.15; 247.
DR   NextBio; 47741; -.
DR   PMAP-CutDB; Q3LXA3; -.
DR   ArrayExpress; Q3LXA3; -.
DR   Bgee; Q3LXA3; -.
DR   CleanEx; HS_DAK; -.
DR   GermOnline; ENSG00000149476; Homo sapiens.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034012; F:FAD-AMP lyase (cyclizing) activity; IEA:EC.
DR   GO; GO:0004371; F:glycerone kinase activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR   InterPro; IPR004006; Dak1.
DR   InterPro; IPR004007; Dak2.
DR   InterPro; IPR012734; DhaK_ATP.
DR   Pfam; PF02733; Dak1; 1.
DR   Pfam; PF02734; Dak2; 1.
DR   TIGRFAMs; TIGR02361; dak_ATP; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cobalt; Complete proteome; FAD; Kinase; Lyase; Magnesium;
KW   Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Polymorphism; Transferase.
FT   CHAIN         1    575       Bifunctional ATP-dependent
FT                                dihydroxyacetone kinase/FAD-AMP lyase
FT                                (cyclizing).
FT                                /FTId=PRO_0000121525.
FT   DOMAIN       18    340       DAK1.
FT   DOMAIN      398    516       DAK2.
FT   NP_BIND     403    407       ATP (By similarity).
FT   NP_BIND     446    494       ATP (By similarity).
FT   ACT_SITE    221    221       Tele-hemiaminal-histidine intermediate
FT                                (By similarity).
FT   METAL       396    396       Magnesium 2 (By similarity).
FT   METAL       401    401       Magnesium 1 (By similarity).
FT   METAL       401    401       Magnesium 2 (By similarity).
FT   METAL       403    403       Magnesium 1 (By similarity).
FT   METAL       404    404       Magnesium 2 (By similarity).
FT   BINDING      59     59       Dihydroxyacetone (By similarity).
FT   BINDING     114    114       Dihydroxyacetone (By similarity).
FT   BINDING     556    556       ATP (By similarity).
FT   VARIANT     185    185       T -> A (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;  58977 MW;  D8C871622535E40D CRC64;
     MTSKKLVNSV AGCADDALAG LVACNPNLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE
     PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL
     AREQARAEGI PVEMVVIGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEIAKQ
     VNVVTKAMGT 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
//