Dihydroxyacetone kinase

Name	Dihydroxyacetone kinase
Synonyms	2.7.1.29 DHA kinase Glycerone kinase
Gene Name	dhaK
Organism	Citrobacter freundii
Amino acid sequence	>lcl\|BSEQ0019095\|Dihydroxyacetone kinase MSQFFFNQRTHLVSDVIDGAIIASPWNNLARLESDPAIRIVVRRDLNKNNVAVISGGGSG HEPAHVGFIGKGMLTAAVCGDVFASPSVDAVLTAIQAVTGEAGCLLIVKNYTGDRLNFGL AAEKARRLGYNVEMLIVGDDISLPDNKHPRGIAGTILVHKIAGYFAERGYNLATVLREAQ YAASNTFSLGVALSSCHLPQETDAAPRHHPGHAELGMGIHGEPGASVIDTQNSAQVVNLM VDKLLAALPETGRLAVMINNLGGVSVAEMAIITRELASSPLHSRIDWLIGPASLVTALDM KGFSLTAIVLEESIEKALLTEVETSNWPTPVPPREITCVVSSHASARVEFQPSANALVAG IVELVTATLSDLETHLNALDAKVGDGDTGSTFAAAAREIASLLHRQQLPLNNLATLFALI GERLTVVMGGSSGVLMSIFFTAAGQKLEQGANVVEALNTGLAQMKFYGGADEGDRTMIDA LQPALTSLLAQPKNLQAAFDAAQAGAERTCLSSKANAGRASYLSSESLLGNMDPGAQRLA MVFKALAESELG
Number of residues	None
Molecular Weight	57939.515
Theoretical pI	5.29
GO Classification	Functions ATP binding lipid binding metal ion binding glycerone kinase activity Processes anaerobic glycerol catabolic process Components
General Function	Metal ion binding
Specific Function	Catalyzes the phosphorylation of dihydroxyacetone.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P45510
UniProtKB Entry Name
Cellular Location	None
Gene sequence	>lcl\|BSEQ0002604\|1659 bp TTAGCCCAGCTCACTCTCCGCTAGCGCTTTAAACACCATCGCTAGGCGCTGCGCGCCGGG GTCCATATTTCCGAGCAGGCTTTCGCTGCTCAGATACGATGCGCGACCCGCATTGGCTTT GCTCGACAAACAGGTTCGTTCGGCTCCCGCTTGCGCGGCGTCGAATGCGGCCTGCAGATT TTTCGGCTGTGCGAGCAGCGAGGTCAGGGCCGGTTGCAGCGCATCAATCATCGTGCGATC GCCTTCGTCTGCGCCGCCGTAGAACTTCATCTGCGCCAGCCCCGTATTTAGCGCTTCGAC AACGTTAGCGCCCTGTTCCAGTTTCTGCCCGGCGGCGGTAAAGAAGATTGACATCAGCAC ACCGCTGGAACCGCCCATCACCACGGTCAGACGTTCGCCAATCAGCGCGAACAGCGTGGC AAGGTTATTCAGCGGCAGCTGCTGGCGATGCAGCAGGCTGGCAATTTCACGCGCCGCGGC GGCAAAGGTCGAACCGGTATCGCCATCGCCGACTTTGGCGTCCAGCGCATTCAGATGAGT CTCCAGATCGGAAAGGGTTGCGGTGACCAGCTCCACAATCCCGGCCACCAGGGCGTTTGC CGAAGGCTGGAATTCCACGCGGGCGCTAGCGTGAGATGACACTACGCAGGTGATTTCACG CGGTGGGACCGGCGTCGGCCAGTTGCTGGTTTCCACTTCGGTGAGCAGTGCTTTTTCGAT GCTCTCTTCCAGCACGATGGCCGTCAGTGAGAAGCCTTTCATATCCAGCGCGGTGACCAG CGAGGCCGGGCCAATTAGCCAGTCGATACGCGAGTGCAGCGGGCTGCTGGCGAGTTCGCG GGTGATGATGGCCATTTCGGCCACGGAAACGCCGCCAAGATTATTAATCATCACCGCCAG ACGACCGGTTTCAGGCAGGGCGGCCAGCAGTTTATCCACCATCAGGTTTACCACTTGCGC ACTGTTTTGGGTGTCGATAACCGATGCGCCTGGTTCGCCGTGAATTCCCATACCCAGCTC CGCATGACCCGGATGATGACGAGGGGCTGCGTCGGTTTCTTGCGGCAGATGACAGCTGGA AAGCGCTACGCCCAGGCTAAAGGTGTTGCTGGCTGCGTACTGCGCTTCACGCAGGACGGT GGCGAGGTTATAGCCGCGTTCGGCAAAATAGCCTGCGATTTTATGCACCAGGATAGTTCC CGCAATGCCACGTGGGTGTTTGTTATCCGGCAGGGAGATGTCGTCGCCGACAATCAGCAT TTCAACGTTATAGCCAAGGCGACGCGCCTTCTCGGCGGCGAGACCGAAATTAAGACGGTC ACCGGTGTAGTTTTTCACAATCAACAAACAGCCAGCCTCACCGGTCACCGCCTGAATCGC GGTCAGTACAGCATCCACGCTCGGGGAGGCGAAAACGTCGCCGCAGACCGCAGCGGTTAG CATGCCTTTACCGATAAACCCAACGTGCGCGGGTTCGTGTCCCGAACCGCCGCCGGAAAT GACCGCTACGTTATTTTTATTAAGGTCACGACGGACCACGATGCGAATGGCCGGATCGCT TTCCAGACGCGCCAGGTTATTCCATGGGCTGGCGATAATCGCCCCGTCGATGACGTCGCT CACAAGATGGGTGCGTTGGTTAAAAAAGAATTGAGACAT
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	Daniel R, Stuertz K, Gottschalk G: Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii. J Bacteriol. 1995 Aug;177(15):4392-401. [7635824 ] Siebold C, Arnold I, Garcia-Alles LF, Baumann U, Erni B: Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain. J Biol Chem. 2003 Nov 28;278(48):48236-44. Epub 2003 Sep 9. [12966101 ]

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