Dihydroxyacetone kinase
Details
- 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
- 552
- Molecular Weight
- 57939.515
- Theoretical pI
- 5.29
- GO Classification
- FunctionsATP binding / glycerone kinase activity / lipid binding / metal ion bindingProcessesanaerobic glycerol catabolic process
- General Function
- Metal ion binding
- Specific Function
- Catalyzes the phosphorylation of dihydroxyacetone.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- 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
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P45510 UniProtKB Entry Name DHAK_CITFR GenBank Protein ID 493083 GenBank Gene ID U09771 - General 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. [Article]
- 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. [Article]