ID   TREF_ECOLC              Reviewed;         549 AA.
AC   B1J0B4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Cytoplasmic trehalase {ECO:0000255|HAMAP-Rule:MF_01059};
DE            EC=3.2.1.28 {ECO:0000255|HAMAP-Rule:MF_01059};
DE   AltName: Full=Alpha,alpha-trehalase {ECO:0000255|HAMAP-Rule:MF_01059};
DE   AltName: Full=Alpha,alpha-trehalose glucohydrolase {ECO:0000255|HAMAP-Rule:MF_01059};
GN   Name=treF {ECO:0000255|HAMAP-Rule:MF_01059}; OrderedLocusNames=EcolC_0198;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes trehalose to glucose. Could be involved, in cells
CC       returning to low osmolarity conditions, in the utilization of the
CC       accumulated cytoplasmic trehalose, which was synthesized in response to
CC       high osmolarity. {ECO:0000255|HAMAP-Rule:MF_01059}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC         glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01059};
CC   -!- PATHWAY: Glycan degradation; trehalose degradation; D-glucose from
CC       alpha,alpha-trehalose: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01059}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01059}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01059}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01059}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000946; ACA75879.1; -; Genomic_DNA.
DR   RefSeq; WP_000934218.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1J0B4; -.
DR   SMR; B1J0B4; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   KEGG; ecl:EcolC_0198; -.
DR   HOGENOM; CLU_006451_3_1_6; -.
DR   OMA; DAPFGWA; -.
DR   UniPathway; UPA00300; UER00535.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071474; P:cellular hyperosmotic response; IEA:InterPro.
DR   GO; GO:0005993; P:trehalose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.50.10.10; -; 1.
DR   HAMAP; MF_01059; Cyt_trehalase; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR023715; Cyt_trehalase.
DR   InterPro; IPR001661; Glyco_hydro_37.
DR   InterPro; IPR018232; Glyco_hydro_37_CS.
DR   PANTHER; PTHR23403; PTHR23403; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   PROSITE; PS00927; TREHALASE_1; 1.
DR   PROSITE; PS00928; TREHALASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosidase; Hydrolase.
FT   CHAIN           1..549
FT                   /note="Cytoplasmic trehalase"
FT                   /id="PRO_1000084457"
FT   ACT_SITE        326
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   ACT_SITE        509
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         175..176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         221..223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         292..294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
FT   BINDING         525
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01059"
SQ   SEQUENCE   549 AA;  63715 MW;  543B83F6BFC1CB9D CRC64;
     MLNQKIQNPN PDELMIEVDL CYELDPYELK LDEMIEAEPE PEMIEGLPAS DALTPADRYL
     ELFEHVQSAK IFPDSKTFPD CAPKMDPLDI LIRYRKVRRH RDFDLRKFVE NHFWLPEVYS
     SEYVSDPQNS LKEHIDQLWP VLTREPQDHI PWSSLLALPQ SYIVPGGRFS ETYYWDSYFT
     MLGLAESGRE DLLKCMADNF AWMIENYGHI PNGNRTYYLS RSQPPVFALM VELFEEDGVR
     GARRYLDHLK MEYAFWMDGA ESLIPNQAYR HVVRMPDGSL LNRYWDDRDT PRDESWLEDV
     ETAKHSGRPP NEVYRDLRAG AASGWDYSSR WLRDTGRLAS IRTTQFIPID LNAFLFKLES
     AIANISALKG EKETEALFRQ KASARRDAVN RYLWDDENGI YRDYDWRREQ LALFSAAAIV
     PLYVGMANHE QADRLANAVR SRLLTPGGIL ASEYETGEQW DKPNGWAPLQ WMAIQGFKMY
     GDDLLGDEIA RSWLKTVNQF YLEQHKMIEK YHIADGVPRE GGGGEYPLQD GFGWTNGVVR
     RLIGLYGEP