ID A6TFC2_KLEP7 Unreviewed; 550 AA. AC A6TFC2; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 02-SEP-2026, entry version 93. DE RecName: Full=Cytoplasmic trehalase {ECO:0000256|HAMAP-Rule:MF_01059}; DE EC=3.2.1.28 {ECO:0000256|HAMAP-Rule:MF_01059}; DE AltName: Full=Alpha,alpha-trehalase {ECO:0000256|HAMAP-Rule:MF_01059}; DE AltName: Full=Alpha,alpha-trehalose glucohydrolase {ECO:0000256|HAMAP-Rule:MF_01059}; GN Name=treF {ECO:0000256|HAMAP-Rule:MF_01059, GN ECO:0000313|EMBL:ABR79256.1}; GN ORFNames=KPN_03869 {ECO:0000313|EMBL:ABR79256.1}; OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Klebsiella; OC Klebsiella pneumoniae complex. OX NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR79256.1, ECO:0000313|Proteomes:UP000000265}; RN [1] {ECO:0000313|EMBL:ABR79256.1, ECO:0000313|Proteomes:UP000000265} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265}; 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:0000256|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:0000256|HAMAP-Rule:MF_01059}; CC -!- PATHWAY: Glycan degradation; trehalose degradation; D-glucose from CC alpha,alpha-trehalose: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01059}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01059}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01059}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. CC {ECO:0000256|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; CP000647; ABR79256.1; -; Genomic_DNA. DR RefSeq; WP_015959116.1; NC_009648.1. DR AlphaFoldDB; A6TFC2; -. DR STRING; 272620.KPN_03869; -. DR PaxDb; 272620-KPN_03869; -. DR EnsemblBacteria; ABR79256; ABR79256; KPN_03869. DR KEGG; kpn:KPN_03869; -. DR HOGENOM; CLU_006451_3_1_6; -. DR UniPathway; UPA00300; UER00535. DR Proteomes; UP000000265; 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-UniRule. DR FunFam; 1.50.10.10:FF:000003; Cytoplasmic trehalase; 1. 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 NCBIfam; NF009773; PRK13270.1; 1. DR NCBIfam; NF009774; PRK13271.1; 1. DR PANTHER; PTHR23403:SF8; CYTOPLASMIC TREHALASE; 1. DR PANTHER; PTHR23403; TREHALASE; 1. DR Pfam; PF01204; Trehalase; 1. DR PRINTS; PR00744; GLHYDRLASE37. DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1. DR PROSITE; PS00927; TREHALASE_1; 1. DR PROSITE; PS00928; TREHALASE_2; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01059}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP- KW Rule:MF_01059}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01059}; KW Reference proteome {ECO:0000313|Proteomes:UP000000265}. FT ACT_SITE 326 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01059" FT ACT_SITE 509 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01059" FT BINDING 168 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01059" FT BINDING 175..176 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01059" FT BINDING 212 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01059" FT BINDING 221..223 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01059" FT BINDING 292..294 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01059" FT BINDING 324 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01059" FT BINDING 525 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01059" SQ SEQUENCE 550 AA; 63737 MW; 650B671D3C96BE6E CRC64; MFSQKLRHVE DDELRIDIDP CYEADPYELK LDEMIDAEPE PEVIEGLPAS DALTPADRYL ELFTNVQKSR IFADSKTFPD CAPKHDPLDI LRNYRKVKRQ PDFDLRQFVE DNFWLPESQS DIYISDPSLT LKEHIDKLWP VLTREPQDHI PWSSLLALPQ AYIVPGGRFS ETYYWDSYFT MLGLAESGRE DLLKCMADNF AWLIETYGHI PNGNRTYYLS RSQPPVFALM VELFEEDGVR GAKRYLDHLK MEHAFWMDGA ESLIPHQAYR HVVRMPDGSL LNRYWDDRDT PRDESWREDV ETARHSGRPA NEVYRDLRAG AASGWDYSSR WLRDITRLAS IRTTQFIPID LNAFLFKLET TIANLSGLKG DRETEAAFRQ KAQDRRAAVN HYLWDDENGC FRDYDWRREQ LALFSAASIV TLYVGLATHE QAERLADAVR ARLLTPGGIM ATEYESGEQW DKPNGWAPLQ WMAIQGFKRY GQDPLGDEIA WSWLQTVNHF YKQHHKLIEK YHIATGVPHE GGGGEYPLQD GFGWTNGVVR RLIGLYGEPT //