ID   ATSK_MYCTO              Reviewed;         295 AA.
AC   P9WKZ0; L0TCF8; P65075; Q50719;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
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=MT3514;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Alpha-ketoglutarate-dependent sulfate ester dioxygenase,
CC       which oxidizes medium-chain alkyl-sulfate esters. Shows preference for
CC       2-ethylhexyl sulfate (2-EHS) in vitro, leading to the formation of
CC       succinate and 2-ethylhexanal. Has likely a role in sulfate scavenging
CC       in vivo. {ECO:0000250|UniProtKB:P9WKZ1}.
CC   -!- FUNCTION: Also causes the inactivation of the 2-carboxyquinoxaline
CC       Ty38c (an antitubercular compound that inhibits DprE1) via oxidative
CC       decarboxylation, using Ty38c instead of alpha-ketoglutarate as a
CC       substrate. Is thus responsible for primary resistance of M.tuberculosis
CC       to Ty38c in vitro. {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; AE000516; AAK47852.1; -; Genomic_DNA.
DR   PIR; C70736; C70736.
DR   RefSeq; WP_003900050.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKZ0; -.
DR   SMR; P9WKZ0; -.
DR   EnsemblBacteria; AAK47852; AAK47852; MT3514.
DR   GeneID; 45427402; -.
DR   KEGG; mtc:MT3514; -.
DR   PATRIC; fig|83331.31.peg.3772; -.
DR   HOGENOM; CLU_036005_2_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; 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   Antibiotic resistance; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..295
FT                   /note="Alpha-ketoglutarate-dependent sulfate ester
FT                   dioxygenase"
FT                   /id="PRO_0000427570"
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