ID   TRES_THETH              Reviewed;         963 AA.
AC   O06458;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Trehalose synthase;
DE            EC=5.4.99.16 {ECO:0000250|UniProtKB:A0R6E0};
DE   AltName: Full=Maltose alpha-D-glucosyltransferase;
GN   Name=treS;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33923 / DSM 674 / AT-62;
RX   PubMed=9042362; DOI=10.1016/s0304-4165(96)00103-1;
RA   Tsusaki K., Nishimoto T., Nakada T., Kubota M., Chaen H., Fukuda S.,
RA   Sugimoto T., Kurimoto M.;
RT   "Cloning and sequencing of trehalose synthase gene from Thermus aquaticus
RT   ATCC33923.";
RL   Biochim. Biophys. Acta 1334:28-32(1997).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of maltose and
CC       alpha,alpha-trehalose by transglucosylation.
CC       {ECO:0000250|UniProtKB:A0R6E0}.
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:A0R6E0};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC       subfamily. {ECO:0000305}.
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DR   EMBL; D86216; BAA19934.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06458; -.
DR   SMR; O06458; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; O06458; -.
DR   BRENDA; 5.4.99.16; 2305.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 2.
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; Isomerase; Metal-binding.
FT   CHAIN           1..963
FT                   /note="Trehalose synthase"
FT                   /id="PRO_0000054344"
FT   ACT_SITE        197
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   ACT_SITE        240
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         201
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   BINDING         202
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   BINDING         204
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   BINDING         305
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
SQ   SEQUENCE   963 AA;  110171 MW;  B6CB3CED365764AE CRC64;
     MDPLWYKDAV IYQLHVRSFF DANNDGYGDF EGLRRKLPYL EELGVNTLWL MPFFQSPLRD
     DGYDISDYYQ ILPVHGTLED FTVDEAHGRG MKVIIELVLN HTSIDHPWFQ EARKPNSPMR
     DWYVWSDTPE KYKGVRVIFK DFETSNWTFD PVAKAYYWHR FYWHQPDLNW DSPEVEKAIH
     QVMFFWADLG VDGFRLDAIP YLYEREGTSC ENLPETIEAV KRLRKALEER YGPGKILLAE
     VNMWPEETLP YFGDGDGVHM AYNFPLMPRI FMALRREDRG PIETMLKEAE GIPETAQWAL
     FLRNHDELTL EKVTEEEREF MYEAYAPDPK FRINLGIRRR LMPLLGGDRR RYELLTALLL
     TLKGTPIVYY GDEIGMGDNP FLGDRNGVRT PMQWSQDRIV AFSRAPYHAL FLPPVSEGPY
     SYHFVNVEAQ RENPHSLLSF NRRFLALRNQ HAKIFGRGSL TLLPVENRRV LAYLREHEGE
     RVLVVANLSR YTQAFDLPLE AYQGLVPVEL FSQQPFPPVE GRYRLTLGPH GFALFALKPV
     EAVLHLPSPD WAEEPAPEEA DLPRVHMPGG PEVLLVDTLV HERGREELLN ALAQTLKEKS
     WLALKPQKVA LLDALRFQKD PPLYLTLLQL ENHRTLQVSL PLLWSPQRRE GPGLFARTHG
     QPGYFYELSL DPGFYRLLLA RLKEGFEGRS LRAYYRGRHP GPVPEAVDLL RPGLAAGEGV
     WVQLGLVQDG GLDRTERVLP RLDLPWVLRP EGGLFWERGA SRRVLALTGS LPPGRPQDLF
     AALEVRLLES LPRLRGHAPG TPGLLPGALH ETEALVRLLG VRLALLHRAL GEVEGVVGGH
     PLLGRGLGAF LELEGEVYLV ALGAEKRGTV EEDLARLAYD VERAVHLALE ALEAELWAFA
     EEVADHLHAA FLQAYRSALP EEALEEAGWT RHMAEVAAEH LHREERPARK RIHERWQAKA
     GKA