TREF_ECO7I
ID TREF_ECO7I Reviewed; 549 AA.
AC B7NNF3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=ECIAI39_4022;
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928164; CAR20133.1; -; Genomic_DNA.
DR RefSeq; WP_000934216.1; NC_011750.1.
DR RefSeq; YP_002409913.1; NC_011750.1.
DR AlphaFoldDB; B7NNF3; -.
DR SMR; B7NNF3; -.
DR STRING; 585057.ECIAI39_4022; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR EnsemblBacteria; CAR20133; CAR20133; ECIAI39_4022.
DR GeneID; 58462844; -.
DR KEGG; ect:ECIAI39_4022; -.
DR PATRIC; fig|585057.6.peg.4163; -.
DR HOGENOM; CLU_006451_3_1_6; -.
DR OMA; DAPFGWA; -.
DR UniPathway; UPA00300; UER00535.
DR Proteomes; UP000000749; 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_1000136401"
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; 63697 MW; 543B82A7FAD4CB9D 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 YLEQHKLIEK YHIADGVPRE GGGGEYPLQD GFGWTNGVVR
RLIGLYGEP
