Q58DK4 (DHAK_BOVIN) 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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	578 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity.
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 By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Contains 1 DhaK domain. Contains 1 DhaL domain.

Ontologies

Keywords
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
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 – 578	578	Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)		PRO_0000121524
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

Sequences

	Sequence		Length	Mass (Da)
	Q58DK4 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 04F870A1C05001E4	FASTA	578	59,124
	10 20 30 40 50 60 MTSKKLVNSV AGCADDALAG LVACNPSLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE 70 80 90 100 110 120 PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL 130 140 150 160 170 180 AREQARAEGI PVEMVVVGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEITDR 190 200 210 220 230 240 VSVVAKAMGT LGVSLSSCSV PGSKPTFELS ADEVELGLGI HGEAGVRRIK MATANEIVAL 250 260 270 280 290 300 MLDHMTSSSN ASHVPVPPGS SVVLMVNNLG GLSFLELGII ADAAVCSLEG HGVKIARALV 310 320 330 340 350 360 GTFMSALEMP GVSLTLLLVD EPLLKLIDAE TTASAWPNVA KVWVTGRKRS RAAPTEPLAA 370 380 390 400 410 420 PDSTTAAGEA SKQMVLVLEW VCTTLLGLEE HLNALDRAAG DGDCGTTHSR AARAIXGWLK 430 440 450 460 470 480 EGPPPASPAQ LLSKLSFLLL EKMGGSSGAL YGLFLTAAAQ PLKAKTDLPA WSAAMDAGLE 490 500 510 520 530 540 AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGANMLQIL TKAVKSAEAA AEATKNMEAG 550 560 570 AGRASYISSA RLDQPDPGAV AAAAILRAIL EVLQSQGA

References

[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BT021593 mRNA. Translation: AAX46440.1.
IPI	IPI00702718.
UniGene	Bt.3266.
3D structure databases
ProteinModelPortal	Q58DK4.
ModBase	Search...
Protein-protein interaction databases
STRING	Q58DK4.
Proteomic databases
PRIDE	Q58DK4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
GeneTree	ENSGT00390000015415.
HOVERGEN	HBG079502.
InParanoid	Q58DK4.
OrthoDB	EOG4PRSQT.
PhylomeDB	Q58DK4.
Family and domain databases
InterPro	IPR004006. Dak1. IPR004007. Dak2. IPR012734. DhaK_ATP. [Graphical view]
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...

Entry information

Entry name

DHAK_BOVIN

Accession

Primary (citable) accession number: Q58DK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	April 26, 2005
Last modified:	September 21, 2011
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program