TREF_SALTI
ID TREF_SALTI Reviewed; 549 AA.
AC Q8Z277;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
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};
GN OrderedLocusNames=STY4200, t3914;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD08022.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71388.1; -; Genomic_DNA.
DR RefSeq; NP_458316.1; NC_003198.1.
DR RefSeq; WP_000934251.1; NZ_WSUR01000001.1.
DR AlphaFoldDB; Q8Z277; -.
DR SMR; Q8Z277; -.
DR STRING; 220341.16505005; -.
DR EnsemblBacteria; AAO71388; AAO71388; t3914.
DR KEGG; stt:t3914; -.
DR KEGG; sty:STY4200; -.
DR PATRIC; fig|220341.7.peg.4289; -.
DR eggNOG; COG1626; Bacteria.
DR HOGENOM; CLU_006451_3_1_6; -.
DR OMA; DAPFGWA; -.
DR UniPathway; UPA00300; UER00535.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000173789"
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; 63678 MW; 889FAD0837C36687 CRC64;
MLNQKLNPTP SEDLTIDVDL FYETDPCELK 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
