ATSK_PSEPU
ID ATSK_PSEPU Reviewed; 301 AA.
AC Q9WWU5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Alpha-ketoglutarate-dependent sulfate ester dioxygenase {ECO:0000303|PubMed:10913158};
DE EC=1.14.11.- {ECO:0000269|PubMed:10913158};
DE AltName: Full=Alkylsulfatase {ECO:0000303|PubMed:10913158};
DE AltName: Full=Type II alkyl sulfatase {ECO:0000303|PubMed:10913158};
GN Name=atsK {ECO:0000303|PubMed:10913158};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6884 / S-313;
RA Vermeij P., Kahnert A., Kertesz M.A.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=DSM 6884 / S-313;
RX PubMed=10913158; DOI=10.1074/jbc.m005820200;
RA Kahnert A., Kertesz M.A.;
RT "Characterization of a sulfur-regulated oxygenative alkylsulfatase from
RT Pseudomonas putida S-313.";
RL J. Biol. Chem. 275:31661-31667(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOGS, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=DSM 6884 / S-313;
RX PubMed=15023059; DOI=10.1021/bi035752v;
RA Muller I., Kahnert A., Pape T., Sheldrick G.M., Meyer-Klaucke W.,
RA Dierks T., Kertesz M., Uson I.;
RT "Crystal structure of the alkylsulfatase AtsK: insights into the catalytic
RT mechanism of the Fe(II) alpha-ketoglutarate-dependent dioxygenase
RT superfamily.";
RL Biochemistry 43:3075-3088(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOGS, COFACTOR, AND SUBUNIT.
RC STRAIN=DSM 6884 / S-313;
RX PubMed=15542595; DOI=10.1074/jbc.m410840200;
RA Muller I., Stuckl C., Wakeley J., Kertesz M., Uson I.;
RT "Succinate complex crystal structures of the alpha-ketoglutarate-dependent
RT dioxygenase AtsK: steric aspects of enzyme self-hydroxylation.";
RL J. Biol. Chem. 280:5716-5723(2005).
CC -!- FUNCTION: Catalyzes the oxygenolytic cleavage of 2-ethylhexyl sulfate
CC (2-EHS) in the presence of alpha-ketoglutarate to yield 2-ethyl-hexanal
CC and succinate, the decarboxylated form of alpha-ketoglutarate. It can
CC accept a wide range of alpha-keto acids including 2-oxo-valerate, 2-
CC oxo-adipate, 2-oxo-octanoate, 3-methyl-2-oxo-butyrate, oxaloacetate-
CC alpha-ketoadipate, and alpha-ketooctanoate. It can catalyze the
CC cleavage of medium-chain alkyl sulfate esters such as butylsulfate,
CC pentylsulfate, hexylsulfate, heptylsulfate, octylsulfate, nonylsulfate,
CC decylsulfate and sodium dodecyl sulfate (SDS).
CC {ECO:0000269|PubMed:10913158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-ethylhexyl sulfate + 2-oxoglutarate + O2 = 2-ethylhexanal +
CC CO2 + H(+) + succinate + sulfate; Xref=Rhea:RHEA:47620,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:87808, ChEBI:CHEBI:87809;
CC Evidence={ECO:0000269|PubMed:10913158};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:10913158, ECO:0000269|PubMed:15023059,
CC ECO:0000269|PubMed:15542595};
CC -!- ACTIVITY REGULATION: Strongly stimulated by ascorbate.
CC {ECO:0000269|PubMed:10913158}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 mM for SDS (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10913158};
CC KM=40 mM for hexylsulfate (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10913158};
CC KM=60 mM for nonylsulfate (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10913158};
CC KM=66 mM for 2-EHS (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10913158};
CC KM=97 mM for decylsulfate (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10913158};
CC KM=140 mM for alpha-ketoglutarate (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10913158};
CC KM=271 mM for heptylsulfate (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10913158};
CC KM=437 mM for octylsulfate (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10913158};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:10913158};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10913158,
CC ECO:0000269|PubMed:15023059, ECO:0000269|PubMed:15542595}.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; AF126201; AAD31784.1; -; Genomic_DNA.
DR PDB; 1OIH; X-ray; 1.89 A; A/B/C/D=1-301.
DR PDB; 1OII; X-ray; 2.19 A; A/B/C/D=1-301.
DR PDB; 1OIJ; X-ray; 2.10 A; A/B/C/D=1-301.
DR PDB; 1OIK; X-ray; 2.06 A; A/D=1-301.
DR PDB; 1VZ4; X-ray; 2.50 A; A/D=1-301.
DR PDB; 1VZ5; X-ray; 2.15 A; A/B/C/D=1-301.
DR PDBsum; 1OIH; -.
DR PDBsum; 1OII; -.
DR PDBsum; 1OIJ; -.
DR PDBsum; 1OIK; -.
DR PDBsum; 1VZ4; -.
DR PDBsum; 1VZ5; -.
DR AlphaFoldDB; Q9WWU5; -.
DR SMR; Q9WWU5; -.
DR DrugBank; DB07518; (2R)-2-ETHYL-1-HEXANESULFONIC ACID.
DR BioCyc; MetaCyc:MON-20686; -.
DR BRENDA; 1.14.11.77; 5092.
DR EvolutionaryTrace; Q9WWU5; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..301
FT /note="Alpha-ketoglutarate-dependent sulfate ester
FT dioxygenase"
FT /id="PRO_0000432470"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15023059"
FT BINDING 108
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:15023059,
FT ECO:0000269|PubMed:15542595"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:15023059,
FT ECO:0000269|PubMed:15542595"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15023059"
FT BINDING 135
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:15023059,
FT ECO:0000269|PubMed:15542595"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:15023059,
FT ECO:0000269|PubMed:15542595"
FT BINDING 275
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:15023059,
FT ECO:0000269|PubMed:15542595"
FT BINDING 279
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:15023059,
FT ECO:0000269|PubMed:15542595"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1OIH"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1OIH"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1VZ4"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1OIH"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1OIH"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:1OIH"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:1OIH"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1OIH"
FT HELIX 224..238
FT /evidence="ECO:0007829|PDB:1OIH"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:1OIH"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:1OIH"
SQ SEQUENCE 301 AA; 33201 MW; ADB169D98E56C71A CRC64;
MSNAALATAP HALELDVHPV AGRIGAEIRG VKLSPDLDAA TVEAIQAALV RHKVIFFRGQ
THLDDQSQEG FAKLLGEPVA HPTVPVVDGT RYLLQLDGAQ GQRANSWHTD VTFVEAYPKA
SILRSVVAPA SGGDTVWANT AAAYQELPEP LRELADKLWA VHSNEYDYAS LKPDIDPAKL
ERHRKVFTST VYETEHPVVR VHPISGERAL QLGHFVKRIK GYSLADSQHL FAVLQGHVTR
LENTVRWRWE AGDVAIWDNR ATQHYAVDDY GTQPRIVRRV TLAGEVPVGV DGQLSRTTRK
G
