ID   TREF_SALDC              Reviewed;         549 AA.
AC   B5FKM4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=SeD_A3978;
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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}.
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DR   EMBL; CP001144; ACH75320.1; -; Genomic_DNA.
DR   RefSeq; WP_000934257.1; NC_011205.1.
DR   AlphaFoldDB; B5FKM4; -.
DR   SMR; B5FKM4; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   KEGG; sed:SeD_A3978; -.
DR   HOGENOM; CLU_006451_3_1_6; -.
DR   OMA; DAPFGWA; -.
DR   UniPathway; UPA00300; UER00535.
DR   Proteomes; UP000008322; Chromosome.
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_1000136409"
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;  63644 MW;  8AC1A83157C36687 CRC64;
     MLNQKLNPTP SEDLTIDVDL LYETDPCELK LDEMIEAEPE PEMIEGLPAS DALTPADRYL
     ELFEHVQSTK LFPDSKTFPD CAPKMDPLDI LIRYRKVRRH RDFDLRRFVE NHFWLPETLS
     SEYVSNPENS LKEHIDQLWP ILTREPQDHI PWSSLLALPQ SYIVPGGRFS ETYYWDSYFT
     MLGLAESGRE DLLKCMADNF AWMIENYGHI PNGNRTYYLS RSQPPVFALM VELFEEDGVR
     GARRYLDHLK MEYAFWMDGA ESLALNQAYR HVVRMPDGSL LNRYWDDRDT PRDESWLEDV
     ETAKHSGRPP NEVYRDLRAG AASGWDYSSR WLRDAGRLAS IRTTQFIPID LNAFLYKLES
     AIANISALKG ERDTEALFRQ KASDRRAAVN HYLWDDENGC YRDYDWRREE MALFSAASIV
     PLYVGMANHE QADRLANVVR SRLLTPGGIM ATEYETGEQW DKPNGWAPLQ WMAIQGFKRY
     GDDMLGDEIA HNWLKTVNHF YQEHHKLIEK YHISGGTPRE GGGGEYPLQD GFGWTNGVVR
     RLIGLYGEP