TREF_SALTY
ID TREF_SALTY Reviewed; 549 AA.
AC Q8ZLC8;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=STM3603;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL22463.1; -; Genomic_DNA.
DR RefSeq; NP_462504.1; NC_003197.2.
DR RefSeq; WP_000934257.1; NC_003197.2.
DR AlphaFoldDB; Q8ZLC8; -.
DR SMR; Q8ZLC8; -.
DR STRING; 99287.STM3603; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR PaxDb; Q8ZLC8; -.
DR EnsemblBacteria; AAL22463; AAL22463; STM3603.
DR GeneID; 1255126; -.
DR KEGG; stm:STM3603; -.
DR PATRIC; fig|99287.12.peg.3808; -.
DR HOGENOM; CLU_006451_3_1_6; -.
DR OMA; DAPFGWA; -.
DR PhylomeDB; Q8ZLC8; -.
DR BioCyc; SENT99287:STM3603-MON; -.
DR UniPathway; UPA00300; UER00535.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IBA:GO_Central.
DR GO; GO:0071474; P:cellular hyperosmotic response; IEA:InterPro.
DR GO; GO:0005993; P:trehalose catabolic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..549
FT /note="Cytoplasmic trehalase"
FT /id="PRO_0000173790"
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
