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
Functions
dioxygenase 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
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
ResourceLink
UniProtKB IDQ9WWU5
UniProtKB Entry NameATSK_PSEPU
GenBank Gene IDAF126201
PDB ID(s)1OIH, 1OII, 1OIJ, 1OIK, 1VZ4, 1VZ5
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]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
(2R)-2-ETHYL-1-HEXANESULFONIC ACIDexperimentalunknowntargetDetails