STF0_MYCS2
ID STF0_MYCS2 Reviewed; 267 AA.
AC A0QQ53;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Trehalose 2-sulfotransferase {ECO:0000305|PubMed:15258569};
DE EC=2.8.2.37 {ECO:0000269|PubMed:15258569};
GN Name=stf0 {ECO:0000303|PubMed:15258569};
GN OrderedLocusNames=MSMEG_0630 {ECO:0000312|EMBL:ABK69637.1},
GN MSMEI_0614 {ECO:0000312|EMBL:AFP37095.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP REACTION MECHANISM, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15866533; DOI=10.1016/j.ab.2005.02.004;
RA Pi N., Hoang M.B., Gao H., Mougous J.D., Bertozzi C.R., Leary J.A.;
RT "Kinetic measurements and mechanism determination of Stf0 sulfotransferase
RT using mass spectrometry.";
RL Anal. Biochem. 341:94-104(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH
RP ALPHA,ALPHA-TREHALOSE, IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE,
RP PATHWAY, SUBUNIT, MUTAGENESIS OF GLU-33 AND GLU-36, AND ACTIVE SITE.
RX PubMed=15258569; DOI=10.1038/nsmb802;
RA Mougous J.D., Petzold C.J., Senaratne R.H., Lee D.H., Akey D.L., Lin F.L.,
RA Munchel S.E., Pratt M.R., Riley L.W., Leary J.A., Berger J.M.,
RA Bertozzi C.R.;
RT "Identification, function and structure of the mycobacterial
RT sulfotransferase that initiates sulfolipid-1 biosynthesis.";
RL Nat. Struct. Mol. Biol. 11:721-729(2004).
CC -!- FUNCTION: Catalyzes the sulfuryl group transfer from 3'-
CC phosphoadenosine-5'-phosphosulfate (PAPS) to trehalose, leading to
CC trehalose-2-sulfate (T2S). The sulfation of trehalose is the first step
CC in the biosynthesis of sulfolipid-1 (SL-1), a major cell wall
CC glycolipid in pathogenic mycobacteria. Cannot use free glucose and
CC unnatural stereoisomers of trehalose (alpha,beta (neo-trehalose) and
CC beta,beta (iso-trehalose)) as substrates.
CC {ECO:0000269|PubMed:15258569}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha,alpha-trehalose = 2-O-
CC sulfo-alpha,alpha-trehalose + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:41608, ChEBI:CHEBI:15378, ChEBI:CHEBI:16551,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:60091; EC=2.8.2.37;
CC Evidence={ECO:0000269|PubMed:15258569};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for 3'-phosphoadenylyl sulfate
CC {ECO:0000269|PubMed:15866533};
CC KM=18 mM for alpha,alpha-trehalose {ECO:0000269|PubMed:15258569};
CC KM=15 mM for alpha,alpha-trehalose {ECO:0000269|PubMed:15866533};
CC Note=kcat is 1.6 sec(-1) (PubMed:15258569). kcat is 134 min(-1)
CC toward trehalose and 96 min(-1) toward PAPS (PubMed:15866533).
CC {ECO:0000269|PubMed:15258569, ECO:0000269|PubMed:15866533};
CC -!- PATHWAY: Glycolipid metabolism. {ECO:0000269|PubMed:15258569}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15258569}.
CC -!- DISRUPTION PHENOTYPE: Loss of trehalose-2-sulfate (T2S) formation.
CC {ECO:0000269|PubMed:15258569}.
CC -!- MISCELLANEOUS: The reaction catalyzed by Stf0 follows a rapid
CC equilibrium random sequential Bi-Bi mechanism with formation of a
CC ternary complex intermediate. {ECO:0000269|PubMed:15866533}.
CC -!- SIMILARITY: Belongs to the Stf0 sulfotransferase family. {ECO:0000305}.
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DR EMBL; CP000480; ABK69637.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37095.1; -; Genomic_DNA.
DR RefSeq; WP_011727079.1; NZ_SIJM01000009.1.
DR RefSeq; YP_885041.1; NC_008596.1.
DR PDB; 1TEX; X-ray; 2.60 A; A/B/C/D=1-267.
DR PDBsum; 1TEX; -.
DR AlphaFoldDB; A0QQ53; -.
DR SMR; A0QQ53; -.
DR STRING; 246196.MSMEI_0614; -.
DR EnsemblBacteria; ABK69637; ABK69637; MSMEG_0630.
DR EnsemblBacteria; AFP37095; AFP37095; MSMEI_0614.
DR GeneID; 66738808; -.
DR KEGG; msg:MSMEI_0614; -.
DR KEGG; msm:MSMEG_0630; -.
DR PATRIC; fig|246196.19.peg.626; -.
DR eggNOG; COG4424; Bacteria.
DR OMA; QEEGWRN; -.
DR OrthoDB; 1016427at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015124; Stf0.
DR InterPro; IPR024628; Sulfotransferase_Stf0_dom.
DR Pfam; PF09037; Sulphotransf; 1.
DR PIRSF; PIRSF021497; Sulphotransferase_Stf0; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Reference proteome; Transferase.
FT CHAIN 1..267
FT /note="Trehalose 2-sulfotransferase"
FT /id="PRO_0000434783"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:15258569"
FT BINDING 14
FT /ligand="alpha,alpha-trehalose"
FT /ligand_id="ChEBI:CHEBI:16551"
FT /evidence="ECO:0000269|PubMed:15258569,
FT ECO:0007744|PDB:1TEX"
FT BINDING 33..39
FT /ligand="alpha,alpha-trehalose"
FT /ligand_id="ChEBI:CHEBI:16551"
FT /evidence="ECO:0000269|PubMed:15258569,
FT ECO:0007744|PDB:1TEX"
FT BINDING 48
FT /ligand="alpha,alpha-trehalose"
FT /ligand_id="ChEBI:CHEBI:16551"
FT /evidence="ECO:0000269|PubMed:15258569,
FT ECO:0007744|PDB:1TEX"
FT BINDING 53
FT /ligand="alpha,alpha-trehalose"
FT /ligand_id="ChEBI:CHEBI:16551"
FT /evidence="ECO:0000269|PubMed:15258569,
FT ECO:0007744|PDB:1TEX"
FT MUTAGEN 33
FT /note="E->A: 4-fold decrease in catalytic efficiency due to
FT a reduction in both trehalose affinity and reaction rate."
FT /evidence="ECO:0000269|PubMed:15258569"
FT MUTAGEN 36
FT /note="E->A: 100-fold decrease in reaction rate and 3-fold
FT increase in trehalose affinity."
FT /evidence="ECO:0000269|PubMed:15258569"
SQ SEQUENCE 267 AA; 30291 MW; 7432364D0ABB8956 CRC64;
MSDHPTAYLV LASQRSGSTL LVESLRATGV AGEPQEFFQY LPNTSMSPQP REWFADVEDQ
SILRLLDPLI EGKPDLAPAT IWRDYIQTVG RTPNGVWGGK LMWNQTPLLV QRAKDLPDRS
GSGLLSAIRD VVGSDPVLIH IHRPDVVSQA VSFWRAVQTR VWRGRPDPVR DARAEYHAGA
IAHVITMLRA QEEGWRAWFT EENVEPIDVD YPYLWRNLTE VVGTVLEALG QDPRLAPKPV
LERQADQRSD EWVERYRRDA QRDGLPL
