ID   B2VCP3_ERWT9            Unreviewed;       554 AA.
AC   B2VCP3;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   18-JUN-2025, entry version 90.
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:CAO98094.1};
GN   OrderedLocusNames=ETA_30480 {ECO:0000313|EMBL:CAO98094.1};
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817 {ECO:0000313|EMBL:CAO98094.1, ECO:0000313|Proteomes:UP000001726};
RN   [1] {ECO:0000313|EMBL:CAO98094.1, ECO:0000313|Proteomes:UP000001726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99
RC   {ECO:0000313|Proteomes:UP000001726};
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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}.
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DR   EMBL; CU468135; CAO98094.1; -; Genomic_DNA.
DR   RefSeq; WP_012442745.1; NC_010694.1.
DR   AlphaFoldDB; B2VCP3; -.
DR   STRING; 465817.ETA_30480; -.
DR   KEGG; eta:ETA_30480; -.
DR   eggNOG; COG1626; Bacteria.
DR   HOGENOM; CLU_006451_3_1_6; -.
DR   UniPathway; UPA00300; UER00535.
DR   Proteomes; UP000001726; 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:UP000001726}.
FT   REGION          295..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        331
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01059"
FT   ACT_SITE        514
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01059"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01059"
FT   BINDING         180..181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01059"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01059"
FT   BINDING         226..228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01059"
FT   BINDING         297..299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01059"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01059"
FT   BINDING         530
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01059"
SQ   SEQUENCE   554 AA;  63467 MW;  1AE4D3477B79DBF0 CRC64;
     MPQAGHQEVF ITFNQNEAMI NTNPVEFEAW HDDYITGPED VGEPHPERIH GLPASDILTP
     SERYQELFTA VQMSRIFSDS KTFADCAPKT DPEPILFRYY LKREQEDFNL LEFVLENFDL
     PDVHDSRYVA DPNHTMAEHI DGLWPVLTRQ PEKHRKFSSL LPLPKPYVVP GGRFSEVYYW
     DSYFSMLGFA AAGRCDLMRS MADNFAWMID KYGHIPNGNR TYYLSRSQPP VFAMMVELFE
     KNDVHEAQHY LPQLKSEYAF WMDGQETLAP NRAHRHVVML SDGSVLNRYW DDRDTPRDES
     YREDVETAGQ SSRPSSEVYR DLRAGAASGW DYTSRWLSEP GRLESIQTTS IVPVDLNALL
     YKLETTIARL SASRGEQATA ERFQQLALRR REAVDRYLWD VQAGLYRDYN WREGEQATFS
     AAAVTPVYVG MASLDQANRT AKAVRDHLLA PGGILCSMSV TGEQWDSPNG WAPVQWMAIK
     GFHSYGDELL AQEIASRWLH TVNSTWQQHH KMVEKYNISG EAALLGGGGE YPLQDGFGWT
     NGVTRRLLEM YPQL
//