Alpha-ketoglutarate-dependent sulfate ester dioxygenase
Details
- Name
- Alpha-ketoglutarate-dependent sulfate ester dioxygenase
- Kind
- protein
- Synonyms
- 1.13.11.-
- Alkylsulfatase
- Type II alkyl sulfatase
- Gene Name
- atsK
- UniProtKB Entry
- Q9WWU5Swiss-Prot
- Organism
- Pseudomonas putida
- NCBI Taxonomy ID
- 303
- Amino acid sequence
>lcl|BSEQ0012221|Alpha-ketoglutarate-dependent sulfate ester dioxygenase MSNAALATAPHALELDVHPVAGRIGAEIRGVKLSPDLDAATVEAIQAALVRHKVIFFRGQ THLDDQSQEGFAKLLGEPVAHPTVPVVDGTRYLLQLDGAQGQRANSWHTDVTFVEAYPKA SILRSVVAPASGGDTVWANTAAAYQELPEPLRELADKLWAVHSNEYDYASLKPDIDPAKL ERHRKVFTSTVYETEHPVVRVHPISGERALQLGHFVKRIKGYSLADSQHLFAVLQGHVTR LENTVRWRWEAGDVAIWDNRATQHYAVDDYGTQPRIVRRVTLAGEVPVGVDGQLSRTTRK G
- Number of residues
- 301
- Molecular Weight
- 33201.21
- Theoretical pI
- 7.06
- GO Classification
- Functionsdioxygenase activity / metal ion binding
- General Function
- Catalyzes the oxygenolytic cleavage of 2-ethylhexyl sulfate (2-EHS) in the presence of alpha-ketoglutarate to yield 2-ethyl-hexanal and succinate, the decarboxylated form of alpha-ketoglutarate. It can accept a wide range of alpha-keto acids including 2-oxo-valerate, 2-oxo-adipate, 2-oxo-octanoate, 3-methyl-2-oxo-butyrate, oxaloacetate-alpha-ketoadipate, and alpha-ketooctanoate. It can catalyze the cleavage of medium-chain alkyl sulfate esters such as butylsulfate, pentylsulfate, hexylsulfate, heptylsulfate, octylsulfate, nonylsulfate, decylsulfate and sodium dodecyl sulfate (SDS).
- Specific Function
- 2-oxoglutarate-dependent dioxygenase activity
- Pfam Domain Function
- TauD (PF02668)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0006213|906 bp TCAGCCTTTACGCGTAGTACGGCTCAGTTGGCCATCCACGCCCACCGGCACTTCACCGGC CAGCGTTACCCGGCGCACGATACGTGGCTGGGTCCCATAATCATCCACCGCGTAGTGCTG TGTCGCACGGTTATCCCAGATAGCCACATCGCCCGCCTCCCAGCGCCAGCGCACGGTGTT CTCAAGGCGCGTGACATGCCCTTGCAGCACCGCGAACAAGTGCTGCGAATCGGCCAGCGA ATAGCCCTTGATGCGTTTGACGAAATGCCCCAGCTGCAGCGCCCGCTCACCGCTGATCGG GTGCACTCGCACCACCGGGTGCTCGGTCTCATACACCGTCGAGGTGAACACTTTGCGATG ACGCTCGAGTTTGGCAGGGTCGATATCGGGCTTGAGGCTGGCATAGTCGTACTCGTTGCT GTGCACCGCCCACAGCTTGTCGGCCAGCTCGCGCAGGGGCTCGGGCAACTCCTGATAGGC CGCAGCGGTATTGGCCCATACAGTATCGCCGCCCGACGCAGGGGCCACCACACTGCGCAG GATCGAGGCCTTGGGGTAGGCCTCTACGAAGGTCACATCGGTGTGCCAGGAGTTGGCCCG CTGCCCTTGGGCGCCATCGAGCTGGAGCAGGTAGCGGGTACCGTCGACCACTGGCACGGT GGGGTGAGCGACCGGCTCGCCCAGCAGCTTGGCAAAACCTTCCTGGCTTTGATCGTCCAG GTGGGTCTGGCCACGGAAGAAGATGACCTTGTGCCGCACCAACGCAGCCTGGATGGCCTC GACTGTGGCGGCATCGAGGTCGGGGGACAGTTTGACCCCGCGTATTTCGGCGCCGATACG GCCGGCGACCGGGTGGACATCAAGTTCGAGGGCGTGCGGCGCGGTGGCCAGTGCAGCGTT GCTCAT
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9WWU5 UniProtKB Entry Name ATSK_PSEPU GenBank Gene ID AF126201 PDB ID(s) 1OIH, 1OII, 1OIJ, 1OIK, 1VZ4, 1VZ5 - General References
- Kahnert A, Kertesz MA: Characterization of a sulfur-regulated oxygenative alkylsulfatase from Pseudomonas putida S-313. J Biol Chem. 2000 Oct 13;275(41):31661-7. [Article]
- Muller I, Kahnert A, Pape T, Sheldrick GM, Meyer-Klaucke W, Dierks T, Kertesz M, Uson I: Crystal structure of the alkylsulfatase AtsK: insights into the catalytic mechanism of the Fe(II) alpha-ketoglutarate-dependent dioxygenase superfamily. Biochemistry. 2004 Mar 23;43(11):3075-88. [Article]
- Muller I, Stuckl C, Wakeley J, Kertesz M, Uson I: Succinate complex crystal structures of the alpha-ketoglutarate-dependent dioxygenase AtsK: steric aspects of enzyme self-hydroxylation. J Biol Chem. 2005 Feb 18;280(7):5716-23. Epub 2004 Nov 12. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details (2R)-2-ETHYL-1-HEXANESULFONIC ACID experimental unknown target Details