ID   TRES_PIMSR              Reviewed;         573 AA.
AC   P72235;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   Pimelobacter sp. (strain R48).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Pimelobacter; unclassified Pimelobacter.
OX   NCBI_TaxID=51662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R48;
RX   PubMed=8645698; DOI=10.1016/0304-4165(96)00023-2;
RA   Tsusaki K., Nishimoto T., Nakada T., Kubota M., Chaen H., Sugimoto T.,
RA   Kurimoto M.;
RT   "Cloning and sequencing of trehalose synthase gene from Pimelobacter sp.
RT   R48.";
RL   Biochim. Biophys. Acta 1290:1-3(1996).
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; D78198; BAA11303.1; -; Genomic_DNA.
DR   PIR; S71450; S71450.
DR   AlphaFoldDB; P72235; -.
DR   SMR; P72235; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   BioCyc; MetaCyc:MON-5647; -.
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; 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; Isomerase; Metal-binding.
FT   CHAIN           1..573
FT                   /note="Trehalose synthase"
FT                   /id="PRO_0000054343"
FT   ACT_SITE        210
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   ACT_SITE        252
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         112
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         180
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         214
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   BINDING         215
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   BINDING         217
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT   BINDING         326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZEU2"
SQ   SEQUENCE   573 AA;  65669 MW;  904990A1A97A1E79 CRC64;
     MSIAESTVLG EEPEWFRTAV FYEVLVRSFR DPNAGGTGDF RGLAEKLDYL QWLGVDCLWV
     PPFFSSPLRD GGYDVADYTG ILPEIGTVED FHAFLDGAHE RGIRVIIDFV MNHTSDAHPW
     FQASRSDPDG PYGDFYVWSD TDELYQDARV IFVDTEPSNW TWDQTRGQYY WHRFFHHQPD
     LNFDNPKVQD AMLEAMAFWL DMGLDGFRLD AVPYLYERPG TNGENLPETH EMLKRVRRFV
     DDNYPDRVLL YEANQWPTDV VEYFGPEERE DGTVVGPESH MAFHFPVMPR IFMAVRRESR
     FPISEIMEQT PAIPEGCQWG IFLRNHDELT LEMVTDEDRD YMWGEYAKDP RMKANIGIRR
     RLAPLLDNDT NQIELFTALL LSLPGSPVLY YGDEIGMGDN IWLGDRDGVR TPMQRTPDRN
     VGFSAATPGK LHLPTIQDPV YGYQSVNVEA QLENPSSLLH WTRRMIHIRR QRDAFGLGTF
     EDLGGSNPAV LSYVRELPGD GGDDVILCVN NLSRFPQPVE LDLRKYEGRV PVELIGGVPF
     PAVGELPYLL TLSGHGFYWF RLTDPDTTGR PVL