ID   ATSK_ACIAD              Reviewed;         317 AA.
AC   Q6FBW1;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Alkylsulfatase {ECO:0000303|Ref.2};
DE            EC=1.14.11.- {ECO:0000269|Ref.2};
GN   Name=atsK {ECO:0000303|Ref.2};
GN   OrderedLocusNames=ACIAD1600 {ECO:0000312|EMBL:CAG68450.1};
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   DOI=10.1002/cctc.201402498;
RA   Baud D., Saaidi P.-L., Monfleur A., Harari M., Cuccaro J., Fossey A.,
RA   Besnard M., Debard A., Mariage A., Pellouin V., Petit J.-L., Salanoubat M.,
RA   Weissenbach J., de Berardinis V., Zaparucha A.;
RT   "Synthesis of mono- and dihydroxylated amino acids with new alpha-
RT   ketoglutarate-dependent dioxygenases: biocatalytic oxidation of C-H
RT   bonds.";
RL   ChemCatChem 6:3012-3017(2014).
CC   -!- FUNCTION: Alpha-ketoglutarate-dependent dioxygenase that in vitro
CC       catalyzes the oxygenolytic release of sulfite from hexylsulfate.
CC       {ECO:0000269|Ref.2}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q9WWU5};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9WWU5}.
CC   -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR   EMBL; CR543861; CAG68450.1; -; Genomic_DNA.
DR   RefSeq; WP_004925066.1; NC_005966.1.
DR   AlphaFoldDB; Q6FBW1; -.
DR   SMR; Q6FBW1; -.
DR   STRING; 62977.ACIAD1600; -.
DR   EnsemblBacteria; CAG68450; CAG68450; ACIAD1600.
DR   GeneID; 45233990; -.
DR   KEGG; aci:ACIAD1600; -.
DR   eggNOG; COG2175; Bacteria.
DR   HOGENOM; CLU_036005_2_1_6; -.
DR   OMA; FVDAYPK; -.
DR   OrthoDB; 1742732at2; -.
DR   BioCyc; ASP62977:ACIAD_RS07345-MON; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
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   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..317
FT                   /note="Alkylsulfatase"
FT                   /id="PRO_0000435698"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
FT   BINDING         105
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
FT   BINDING         132
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
FT   BINDING         261
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
FT   BINDING         272
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
FT   BINDING         276
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
SQ   SEQUENCE   317 AA;  35749 MW;  86BBE9868DF55E7D CRC64;
     MTTFIQNPTQ QLQLRKLTGR IGAEISGIHL SSELDSSTVQ FIHDALLEHK VLFFRGQQHL
     GDTEQEKFAE LFGSPVKHPT VPAADGTDFI FELDSQKGAR ANSWHTDVTF VDAYPKISIL
     RGLIIPETGG DTTWANTETA YEDLPELLKQ FAEQLVAVHS NEYDYGGPKQ NVEPEQLERL
     KKVFVSTKYE TEHPVVIVHP ETGKKSLLLG HFFKRLVGFS QSDSQLLFNI LQEKVTRPEN
     TVRWQWQEGD VVIWDNRSTQ HYAVNDYGDQ HRVVRRITLA GEVTTGAHGL KGKTTLPKDL
     SAEQLEKAKL HAVLNAN