ID   ATSK_MYCBO              Reviewed;         295 AA.
AC   P65076; A0A1R3Y490; Q50719; X2BPH3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Alpha-ketoglutarate-dependent sulfate ester dioxygenase {ECO:0000250|UniProtKB:P9WKZ1};
DE            EC=1.14.11.- {ECO:0000250|UniProtKB:P9WKZ1};
DE   AltName: Full=Type II alkyl sulfatase {ECO:0000250|UniProtKB:P9WKZ1};
GN   OrderedLocusNames=BQ2027_MB3440;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Alpha-ketoglutarate-dependent sulfate ester dioxygenase,
CC       which oxidizes medium-chain alkyl-sulfate esters. Thus, catalyzes the
CC       oxygenolytic cleavage of 2-ethylhexyl sulfate (2-EHS), leading to the
CC       formation of succinate and 2-ethylhexanal. Has likely a role in sulfate
CC       scavenging in vivo. {ECO:0000250|UniProtKB:P9WKZ1}.
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:0000250|UniProtKB:P9WKZ1};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:P9WKZ1};
CC   -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU02068.1; -; Genomic_DNA.
DR   RefSeq; NP_857080.1; NC_002945.3.
DR   RefSeq; WP_003900050.1; NC_002945.4.
DR   AlphaFoldDB; P65076; -.
DR   SMR; P65076; -.
DR   EnsemblBacteria; SIU02068; SIU02068; BQ2027_MB3440.
DR   GeneID; 45427402; -.
DR   PATRIC; fig|233413.5.peg.3775; -.
DR   OMA; FVDAYPK; -.
DR   Proteomes; UP000001419; Chromosome.
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   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..295
FT                   /note="Alpha-ketoglutarate-dependent sulfate ester
FT                   dioxygenase"
FT                   /id="PRO_0000104126"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
FT   BINDING         98
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ1"
FT   BINDING         100
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ1"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
FT   BINDING         125
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
FT   BINDING         252
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKZ1"
FT   BINDING         263
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
FT   BINDING         267
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WWU5"
SQ   SEQUENCE   295 AA;  32579 MW;  213EB93DEF58F2A6 CRC64;
     MTDLITVKKL GSRIGAQIDG VRLGGDLDPA AVNEIRAALL AHKVVFFRGQ HQLDDAEQLA
     FAGLLGTPIG HPAAIALADD APIITPINSE FGKANRWHTD VTFAANYPAA SVLRAVSLPS
     YGGSTLWANT AAAYAELPEP LKCLTENLWA LHTNRYDYVT TKPLTAAQRA FRQVFEKPDF
     RTEHPVVRVH PETGERTLLA GDFVRSFVGL DSHESRVLFE VLQRRITMPE NTIRWNWAPG
     DVAIWDNRAT QHRAIDDYDD QHRLMHRVTL MGDVPVDVYG QASRVISGAP MEIAG