TRES_MYCTO
ID TRES_MYCTO Reviewed; 601 AA.
AC P9WQ18; L0T5R2; O07176; Q7DAF7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Trehalose synthase/amylase TreS {ECO:0000250|UniProtKB:P9WQ19};
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P9WQ19};
DE EC=5.4.99.16 {ECO:0000250|UniProtKB:P9WQ19};
DE AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000250|UniProtKB:P9WQ19};
DE Short=MTase {ECO:0000250|UniProtKB:P9WQ19};
GN Name=treS {ECO:0000250|UniProtKB:P9WQ19}; OrderedLocusNames=MT0134;
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: Catalyzes the reversible interconversion of maltose and
CC trehalose by transglucosylation. Also displays amylase activity,
CC catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC glycogen and maltooligosaccharides such as maltoheptaose, to produce
CC maltose which then can be converted to trehalose. TreS plays a key role
CC in the utilization of trehalose for the production of glycogen and
CC alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of
CC maltose-1-phosphate (M1P). Might also function as a sensor and/or
CC regulator of trehalose levels within the cell. Thus, when trehalose
CC levels in the cell become dangerously low, TreS could expedite the
CC conversion of glycogen to maltose via its amylase activity and then
CC convert the maltose to trehalose; but this enzyme also could expedite
CC or promote the conversion of trehalose to glycogen when cytoplasmic
CC trehalose levels become too high. {ECO:0000250|UniProtKB:P9WQ19}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC Evidence={ECO:0000250|UniProtKB:P9WQ19};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P9WQ19};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000250|UniProtKB:P9WQ19}.
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000250|UniProtKB:P9WQ19}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:A0R6E0}.
CC -!- MISCELLANEOUS: Maltose-1-phosphate (M1P), the building block required
CC for alpha-glucan production, is generated by two alternative routes:
CC the TreS-Pep2 branch and the GlgC-GlgM branch, however it seems that
CC TreS-Pep2 branch provides most of M1P for the GlgE pathway in
CC M.tuberculosis. {ECO:0000250|UniProtKB:P9WQ19}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000516; AAK44358.1; -; Genomic_DNA.
DR PIR; G70983; G70983.
DR RefSeq; WP_003400893.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQ18; -.
DR SMR; P9WQ18; -.
DR BindingDB; P9WQ18; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAK44358; AAK44358; MT0134.
DR GeneID; 45424092; -.
DR KEGG; mtc:MT0134; -.
DR PATRIC; fig|83331.31.peg.144; -.
DR HOGENOM; CLU_006462_2_1_11; -.
DR UniPathway; UPA00164; -.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR InterPro; IPR012810; TreS/a-amylase_N.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR TIGRFAMs; TIGR02456; treS_nterm; 1.
PE 3: Inferred from homology;
KW Calcium; Capsule biogenesis/degradation; Carbohydrate metabolism;
KW Glycogen biosynthesis; Glycogen metabolism; Glycosidase; Hydrolase;
KW Isomerase; Metal-binding; Polysaccharide degradation.
FT CHAIN 1..601
FT /note="Trehalose synthase/amylase TreS"
FT /id="PRO_0000426853"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT ACT_SITE 280
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
SQ SEQUENCE 601 AA; 68593 MW; FE52E5258F38116E CRC64;
MNEAEHSVEH PPVQGSHVEG GVVEHPDAKD FGSAAALPAD PTWFKHAVFY EVLVRAFFDA
SADGSGDLRG LIDRLDYLQW LGIDCIWLPP FYDSPLRDGG YDIRDFYKVL PEFGTVDDFV
ALVDAAHRRG IRIITDLVMN HTSESHPWFQ ESRRDPDGPY GDYYVWSDTS ERYTDARIIF
VDTEESNWSF DPVRRQFYWH RFFSHQPDLN YDNPAVQEAM IDVIRFWLGL GIDGFRLDAV
PYLFEREGTN CENLPETHAF LKRVRKVVDD EFPGRVLLAE ANQWPGDVVE YFGDPNTGGD
ECHMAFHFPL MPRIFMAVRR ESRFPISEII AQTPPIPDMA QWGIFLRNHD ELTLEMVTDE
ERDYMYAEYA KDPRMKANVG IRRRLAPLLD NDRNQIELFT ALLLSLPGSP VLYYGDEIGM
GDVIWLGDRD GVRIPMQWTP DRNAGFSTAN PGRLYLPPSQ DPVYGYQAVN VEAQRDTSTS
LLNFTRTMLA VRRRHPAFAV GAFQELGGSN PSVLAYVRQV AGDDGDTVLC VNNLSRFPQP
IELDLQQWTN YTPVELTGHV EFPRIGQVPY LLTLPGHGFY WFQLTTHEVG APPTCGGERR
L
