GLST_MYCTO
ID GLST_MYCTO Reviewed; 326 AA.
AC P9WGB8; L0T6N8; P71801; Q8VK27;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Glycolipid sulfotransferase MT1418;
DE EC=2.8.2.-;
GN OrderedLocusNames=MT1418;
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: Involved in the synthesis of cell wall sulfolipids with
CC activity towards mycobacterial trehalose glycolipids and eukaryotic
CC glycolipids such as glucosylceramide and galactosylceramide (type I and
CC II) but not towards eukaryotic 3'-sulfate galactosylceramide.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK45682.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK45682.1; ALT_INIT; Genomic_DNA.
DR PIR; B70958; B70958.
DR RefSeq; WP_003917467.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGB8; -.
DR SMR; P9WGB8; -.
DR EnsemblBacteria; AAK45682; AAK45682; MT1418.
DR KEGG; mtc:MT1418; -.
DR PATRIC; fig|83331.31.peg.1525; -.
DR HOGENOM; CLU_027239_3_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW Transferase.
FT CHAIN 1..326
FT /note="Glycolipid sulfotransferase MT1418"
FT /id="PRO_0000428389"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 40..45
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 116..124
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
SQ SEQUENCE 326 AA; 36975 MW; CBFE3A729E3A1086 CRC64;
MNSEHPMTDR VVYRSLMADN LRWDALQLRD GDIIISAPSK SGLTWTQRLV SLLVFDGPDL
PGPLSTVSPW LDQTIRPIEE VVATLDAQQH RRFIKTHTPL DGLVLDDRVS YICVGRDPRD
AAVSMLYQSA NMNEDRMRIL HEAVVPFHER IAPPFAELGH ARSPTEEFRD WMEGPNPPPP
GIGFTHLKGI GTLANILHQL GTVWVRRHLP NVALFHYADY QADLAGELLR PARVLGIAAT
RDRARDLAQY ATLDAMRSRA SEIAPNTTDG IWHSDERFFR RGGSGDWQQF FTEAEHLRYY
HRINQLAPPD LLAWAHEGRR GYDPAN