Q3LXA3 (DHAK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)

Including the following 2 domains:

1. ATP-dependent dihydroxyacetone kinase
   Short name=DHA kinase
   EC=2.7.1.29
   Alternative name(s):
   Glycerone kinase
2. FAD-AMP lyase (cyclizing)
   EC=4.6.1.15
   Alternative name(s):
   FAD-AMP lyase (cyclic FMN forming)
   FMN cyclase

Gene names

Name:

DAK

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes both the phosphorylation of dihydroxyacetone and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Ref.1
Catalytic activity	ATP + glycerone = ADP + glycerone phosphate. FAD = AMP + riboflavin cyclic-4',5'-phosphate.
Cofactor	Magnesium By similarity. Manganese or cobalt; for FAD-AMP lyase activity By similarity.
Enzyme regulation	Each activity is inhibited by the substrate(s) of the other.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the dihydroxyacetone kinase (DAK) family. Contains 1 DhaK domain. Contains 1 DhaL domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Cobalt FAD Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Lyase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	glycerol metabolic process Inferred from electronic annotation. Source: InterPro innate immune response Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW FAD-AMP lyase (cyclizing) activity Inferred from electronic annotation. Source: EC glycerone kinase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 575	575	Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)		PRO_0000121525
Regions
	Domain	9 – 336	328	DhaK
	Domain	372 – 571	200	DhaL
	Nucleotide binding	401 – 404	4	ATP By similarity
	Nucleotide binding	446 – 447	2	ATP By similarity
	Nucleotide binding	494 – 495	2	ATP By similarity
	Nucleotide binding	556 – 558	3	ATP By similarity
	Region	56 – 59	4	Dihydroxyacetone binding By similarity
Sites
	Active site	221	1	Tele-hemiaminal-histidine intermediate By similarity
	Binding site	109	1	Dihydroxyacetone By similarity
	Binding site	114	1	Dihydroxyacetone By similarity
	Binding site	486	1	ATP; via carbonyl oxygen By similarity
Natural variations
	Natural variant	185	1	A → T. Ref.1 Ref.2 Ref.3 Corresponds to variant rs2260655 [ dbSNP | Ensembl ].		VAR_028108
	Natural variant	334	1	A → G. Corresponds to variant rs35723406 [ dbSNP | Ensembl ].		VAR_054780
Experimental info
	Sequence conflict	7	1	V → A in BAB14722. Ref.2
	Sequence conflict	19	1	A → S in BAD97300. Ref.3
	Sequence conflict	75	1	V → A in BAB14722. Ref.2
	Sequence conflict	376	1	L → P in BAB14722. Ref.2
	Sequence conflict	497	1	D → G in BAB14722. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q3LXA3 [UniParc]. Last modified November 2, 2010. Version 2. Checksum: 4DB8C5326F65122C	FASTA	575	58,947
	10 20 30 40 50 60 MTSKKLVNSV AGCADDALAG LVACNPNLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE 70 80 90 100 110 120 PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL 130 140 150 160 170 180 AREQARAEGI PVEMVVIGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEIAKQ 190 200 210 220 230 240 VNVVAKAMGT LGVSLSSCSV PGSKPTFELS ADEVELGLGI HGEAGVRRIK MATADEIVKL 250 260 270 280 290 300 MLDHMTNTTN ASHVPVQPGS SVVMMVNNLG GLSFLELGII ADATVRSLEG RGVKIARALV 310 320 330 340 350 360 GTFMSALEMP GISLTLLLVD EPLLKLIDAE TTAAAWPNVA AVSITGRKRS RVAPAEPQEA 370 380 390 400 410 420 PDSTAAGGSA SKRMALVLER VCSTLLGLEE HLNALDRAAG DGDCGTTHSR AARAIQEWLK 430 440 450 460 470 480 EGPPPASPAQ LLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKAKTSLPA WSAAMDAGLE 490 500 510 520 530 540 AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGADLLQVL TKAVKSAEAA AEATKNMEAG 550 560 570 AGRASYISSA RLEQPDPGAV AAAAILRAIL EVLQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases." Cabezas A., Costas M.J., Pinto R.M., Couto A., Cameselle J.C. Biochem. Biophys. Res. Commun. 338:1682-1689(2005) [PubMed: 16289032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FAD-AMP LYASE ACTIVITY, VARIANT THR-185. Tissue: Brain.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-185. Tissue: Thyroid.
[3]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-185. Tissue: Kidney.
[4]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ138290 mRNA. Translation: ABA10576.1. AK023915 mRNA. Translation: BAB14722.1. AK223580 mRNA. Translation: BAD97300.1. AP003108 Genomic DNA. No translation available. BC001341 mRNA. Translation: AAH01341.1.
IPI	IPI00551024.
RefSeq	NP_056348.2. NM_015533.3.
UniGene	Hs.6278.
3D structure databases
ProteinModelPortal	Q3LXA3.
SMR	Q3LXA3. Positions 1-572.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3LXA3.
PTM databases
PhosphoSite	Q3LXA3.
Polymorphism databases
DMDM	311033370.
2D gel databases
REPRODUCTION-2DPAGE	IPI00551024.
Proteomic databases
PRIDE	Q3LXA3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000311463; ENSP00000310493; ENSG00000149476. ENST00000394900; ENSP00000378360; ENSG00000149476.
GeneID	26007.
KEGG	hsa:26007.
UCSC	uc001nre.1. human.
Organism-specific databases
CTD	26007.
GeneCards	GC11P061100.
HGNC	HGNC:24552. DAK.
HPA	HPA039486.
neXtProt	NX_Q3LXA3.
PharmGKB	PA142672014.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG473357.
HOVERGEN	HBG079502.
InParanoid	Q3LXA3.
OMA	GFVGPGL.
OrthoDB	EOG4PRSQT.
PhylomeDB	Q3LXA3.
Enzyme and pathway databases
BRENDA	2.7.1.29. 2681.
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q3LXA3.
Bgee	Q3LXA3.
CleanEx	HS_DAK.
Genevestigator	Q3LXA3.
GermOnline	ENSG00000149476. Homo sapiens.
Family and domain databases
InterPro	IPR004006. Dak1. IPR004007. Dak2. IPR012734. DhaK_ATP. [Graphical view]
KO	K00863.
Pfam	PF02733. Dak1. 1 hit. PF02734. Dak2. 1 hit. [Graphical view]
SUPFAM	SSF101473. Dak2. 1 hit.
TIGRFAMs	TIGR02361. Dak_ATP. 1 hit.
PROSITE	PS51481. DHAK. 1 hit. PS51480. DHAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	47741.
PMAP-CutDB	Q3LXA3.

Entry information

Entry name

DHAK_HUMAN

Accession

Primary (citable) accession number: Q3LXA3
Secondary accession number(s): Q53EQ9, Q9BVA7, Q9H895

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	November 2, 2010
Last modified:	January 25, 2012
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.