Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha-ketoglutarate-dependent sulfate ester dioxygenase

Gene

atsK

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

2-ethylhexyl sulfate + alpha-ketoglutarate + O2 = 2-ethyl-hexanal + succinate + CO2 + sulfate.1 Publication

Cofactori

Fe2+3 Publications

Enzyme regulationi

Strongly stimulated by ascorbate.1 Publication

Kineticsi

  1. KM=34 mM for SDS (at pH 7 and 30 degrees Celsius)1 Publication
  2. KM=40 mM for hexylsulfate (at pH 7 and 30 degrees Celsius)1 Publication
  3. KM=60 mM for nonylsulfate (at pH 7 and 30 degrees Celsius)1 Publication
  4. KM=66 mM for 2-EHS (at pH 7 and 30 degrees Celsius)1 Publication
  5. KM=97 mM for decylsulfate (at pH 7 and 30 degrees Celsius)1 Publication
  6. KM=140 mM for alpha-ketoglutarate (at pH 7 and 30 degrees Celsius)1 Publication
  7. KM=271 mM for heptylsulfate (at pH 7 and 30 degrees Celsius)1 Publication
  8. KM=437 mM for octylsulfate (at pH 7 and 30 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 7.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei81 – 811Substrate1 Publication
    Metal bindingi108 – 1081Iron2 Publications
    Metal bindingi110 – 1101Iron2 Publications
    Binding sitei111 – 1111Substrate; via amide nitrogen1 Publication
    Binding sitei135 – 13512-oxoglutarate2 Publications
    Metal bindingi264 – 2641Iron2 Publications
    Binding sitei275 – 27512-oxoglutarate2 Publications
    Binding sitei279 – 27912-oxoglutarate2 Publications

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-ketoglutarate-dependent sulfate ester dioxygenase1 Publication (EC:1.14.11.-1 Publication)
    Alternative name(s):
    Alkylsulfatase1 Publication
    Type II alkyl sulfatase1 Publication
    Gene namesi
    Name:atsK1 Publication
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 301301Alpha-ketoglutarate-dependent sulfate ester dioxygenasePRO_0000432470Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.3 Publications

    Structurei

    Secondary structure

    1
    301
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 249Combined sources
    Beta strandi26 – 305Combined sources
    Helixi39 – 5214Combined sources
    Beta strandi53 – 575Combined sources
    Helixi65 – 739Combined sources
    Beta strandi78 – 814Combined sources
    Beta strandi94 – 963Combined sources
    Turni110 – 1134Combined sources
    Beta strandi114 – 1163Combined sources
    Beta strandi119 – 1279Combined sources
    Beta strandi135 – 1395Combined sources
    Helixi140 – 1456Combined sources
    Helixi149 – 1579Combined sources
    Beta strandi159 – 1635Combined sources
    Beta strandi193 – 2019Combined sources
    Turni203 – 2053Combined sources
    Beta strandi208 – 2103Combined sources
    Beta strandi216 – 2194Combined sources
    Helixi224 – 23815Combined sources
    Helixi241 – 2433Combined sources
    Beta strandi244 – 2474Combined sources
    Beta strandi254 – 2585Combined sources
    Beta strandi261 – 2666Combined sources
    Beta strandi276 – 2827Combined sources
    Beta strandi296 – 2994Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OIHX-ray1.89A/B/C/D1-301[»]
    1OIIX-ray2.19A/B/C/D1-301[»]
    1OIJX-ray2.10A/B/C/D1-301[»]
    1OIKX-ray2.06A/D1-301[»]
    1VZ4X-ray2.50A/D1-301[»]
    1VZ5X-ray2.15A/B/C/D1-301[»]
    ProteinModelPortaliQ9WWU5.
    SMRiQ9WWU5. Positions 13-300.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9WWU5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TfdA dioxygenase family.Curated

    Family and domain databases

    InterProiIPR003819. TauD/TfdA-like.
    [Graphical view]
    PfamiPF02668. TauD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9WWU5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSNAALATAP HALELDVHPV AGRIGAEIRG VKLSPDLDAA TVEAIQAALV
    60 70 80 90 100
    RHKVIFFRGQ THLDDQSQEG FAKLLGEPVA HPTVPVVDGT RYLLQLDGAQ
    110 120 130 140 150
    GQRANSWHTD VTFVEAYPKA SILRSVVAPA SGGDTVWANT AAAYQELPEP
    160 170 180 190 200
    LRELADKLWA VHSNEYDYAS LKPDIDPAKL ERHRKVFTST VYETEHPVVR
    210 220 230 240 250
    VHPISGERAL QLGHFVKRIK GYSLADSQHL FAVLQGHVTR LENTVRWRWE
    260 270 280 290 300
    AGDVAIWDNR ATQHYAVDDY GTQPRIVRRV TLAGEVPVGV DGQLSRTTRK

    G
    Length:301
    Mass (Da):33,201
    Last modified:November 1, 1999 - v1
    Checksum:iADB169D98E56C71A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF126201 Genomic DNA. Translation: AAD31784.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF126201 Genomic DNA. Translation: AAD31784.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OIHX-ray1.89A/B/C/D1-301[»]
    1OIIX-ray2.19A/B/C/D1-301[»]
    1OIJX-ray2.10A/B/C/D1-301[»]
    1OIKX-ray2.06A/D1-301[»]
    1VZ4X-ray2.50A/D1-301[»]
    1VZ5X-ray2.15A/B/C/D1-301[»]
    ProteinModelPortaliQ9WWU5.
    SMRiQ9WWU5. Positions 13-300.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9WWU5.

    Family and domain databases

    InterProiIPR003819. TauD/TfdA-like.
    [Graphical view]
    PfamiPF02668. TauD. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. Vermeij P., Kahnert A., Kertesz M.A.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DSM 6884 / S-313.
    2. "Characterization of a sulfur-regulated oxygenative alkylsulfatase from Pseudomonas putida S-313."
      Kahnert A., Kertesz M.A.
      J. Biol. Chem. 275:31661-31667(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR, SUBUNIT, SUBSTRATE SPECIFICITY.
      Strain: DSM 6884 / S-313.
    3. "Crystal structure of the alkylsulfatase AtsK: insights into the catalytic mechanism of the Fe(II) alpha-ketoglutarate-dependent dioxygenase superfamily."
      Muller I., Kahnert A., Pape T., Sheldrick G.M., Meyer-Klaucke W., Dierks T., Kertesz M., Uson I.
      Biochemistry 43:3075-3088(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE ANALOGS, COFACTOR, SUBUNIT, REACTION MECHANISM.
      Strain: DSM 6884 / S-313.
    4. "Succinate complex crystal structures of the alpha-ketoglutarate-dependent dioxygenase AtsK: steric aspects of enzyme self-hydroxylation."
      Muller I., Stuckl C., Wakeley J., Kertesz M., Uson I.
      J. Biol. Chem. 280:5716-5723(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE ANALOGS, COFACTOR, SUBUNIT.
      Strain: DSM 6884 / S-313.

    Entry informationi

    Entry nameiATSK_PSEPU
    AccessioniPrimary (citable) accession number: Q9WWU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 2015
    Last sequence update: November 1, 1999
    Last modified: March 16, 2016
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.