ID   DHAK_RAT                Reviewed;         578 AA.
AC   Q4KLZ6;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Brown Norway; TISSUE=Testis;
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   [2]
RP   FUNCTION, AND FAD-AMP LYASE ACTIVITY.
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   [3]
RP   COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11695920; DOI=10.1021/bi0157159;
RA   Cabezas A., Pinto R.M., Fraiz F., Canales J., Gonzalez-Santiago S.,
RA   Cameselle J.C.;
RT   "Purification, characterization, and substrate and inhibitor
RT   structure-activity studies of rat liver FAD-AMP lyase (cyclizing):
RT   preference for FAD and specificity for splitting ribonucleoside
RT   diphosphate-X into ribonucleotide and a five-atom cyclic
RT   phosphodiester of X, either a monocyclic compound or a cis-bicyclic
RT   phosphodiester-pyranose fusion.";
RL   Biochemistry 40:13710-13722(2001).
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.
CC   -!- ENZYME REGULATION: Each activity is inhibited by the substrate(s)
CC       of the other.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8.8 uM for FAD with manganese;
CC         KM=12.5 uM for ADP-glucose with manganese;
CC         KM=652 uM for UDP-glucose with manganese;
CC         KM=606 uM for UDP-galactose with manganese;
CC         KM=714 uM for UDP-xylose with manganese;
CC         KM=107 uM for UDP-glucuronate with manganese;
CC         KM=108 uM for UDP-galacturonate with manganese;
CC         KM=416 uM for CDP-glucose with manganese;
CC         KM=795 uM for CDP-glycerol with manganese;
CC         KM=784 uM for GDP-glucose with manganese;
CC         KM=343 uM for GDP-alpha-L-fucose with manganese;
CC         KM=114 uM for FAD with cobalt;
CC         KM=120 uM for ADP-glucose with cobalt;
CC         KM=2550 uM for UDP-glucose with cobalt;
CC         KM=3661 uM for UDP-galactose with cobalt;
CC         KM=2354 uM for UDP-xylose with cobalt;
CC         KM=539 uM for UDP-glucuronate with cobalt;
CC         KM=759 uM for UDP-galacturonate with cobalt;
CC         KM=3703 uM for CDP-glucose with cobalt;
CC         KM=2031 uM for CDP-glycerol with cobalt;
CC         KM=2246 uM for GDP-glucose with cobalt;
CC         KM=991 uM for GDP-alpha-L-fucose with cobalt;
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; BC098925; AAH98925.1; -; mRNA.
DR   IPI; IPI00372498; -.
DR   RefSeq; NP_001034120.1; -.
DR   UniGene; Rn.55630; -.
DR   PRIDE; Q4KLZ6; -.
DR   Ensembl; ENSRNOG00000020704; Rattus norvegicus.
DR   GeneID; 361730; -.
DR   KEGG; rno:361730; -.
DR   NMPDR; fig|10116.3.peg.3721; -.
DR   RGD; 1311026; Dak.
DR   HOVERGEN; Q4KLZ6; -.
DR   BRENDA; 2.7.1.29; 248.
DR   NextBio; 677430; -.
DR   ArrayExpress; Q4KLZ6; -.
DR   GermOnline; ENSRNOG00000020704; Rattus norvegicus.
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; FAD; Kinase; Lyase; Magnesium; Manganese;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    578       Bifunctional ATP-dependent
FT                                dihydroxyacetone kinase/FAD-AMP lyase
FT                                (cyclizing).
FT                                /FTId=PRO_0000121527.
FT   DOMAIN       18    340       DAK1.
FT   DOMAIN      398    571       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       403    403       Magnesium 2 (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).
SQ   SEQUENCE   578 AA;  59444 MW;  C343482447F9770B CRC64;
     MSSKKMVNSV EGCAGDALAG FVACNPDLQL LQGYRVALRS DLDSLKGRVA LLSGGGSGHE
     PAHAGFIGKG MLTGVIAGAV FASPAVGSIL AAIRAVAQAG TAGTLLIVKN YTGDRLNFGL
     AMEQAKAEGI SVEMVVIEDD SAFTVLKKAG RRGLCGTILI HKVAGALAEE GMGLEEITKK
     VSVIAKAIGT LGVSLSPCSV PGTKPTFELA ADEMELGLGI HGEAGVRRIK LVPVDQIVTL
     MLDHMTDTSN ISHVPVKSGS SVVLMVNNLG GLSFLELGII ADAAIRLLEG RGVKVARALV
     GTFMSALEMR GVSLTLMLVD EPLLKLIDAE TNAKAWPHMS KVSVTGRNRI RAAPTEPAEA
     PEATAAGGVA SKQMTLVLDR ISTTLIGLEE HLNALDRAAG DGDCGSTHSR AAKAIQGWLK
     EGPTPASPAQ VLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKANTDLPA WSAAMDAGLK
     AMQKYGKAAP GDRTMLDSLW AAAQELQAWK SPGASLLPVL TKAVKSAEAA AEATKNMEAG
     AGRASYISSA QLDQPDPGAV AAAAIFRAIL EVLQTKAA
//