Alpha-ketoglutarate-dependent sulfate ester dioxygenase

Details

Name
Alpha-ketoglutarate-dependent sulfate ester dioxygenase
Synonyms
  • 1.13.11.-
  • Alkylsulfatase
  • Type II alkyl sulfatase
Gene Name
atsK
Organism
Pseudomonas putida
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
Functions
dioxygenase activity / metal ion binding
General Function
Metal ion binding
Specific Function
Catalyzes the oxigenolytic 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).
Pfam Domain Function
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
ResourceLink
UniProtKB IDQ9WWU5
UniProtKB Entry NameATSK_PSEPU
GenBank Gene IDAF126201
General References
  1. 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]
  2. 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]
  3. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB07518(2R)-2-ETHYL-1-HEXANESULFONIC ACIDexperimentalunknownDetails