TREA_APIME
ID TREA_APIME Reviewed; 626 AA.
AC A8J4S9; P85151;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Trehalase;
DE EC=3.2.1.28;
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE Flags: Precursor;
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7460;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAF81545.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-54; 128-147; 157-188;
RP 220-239; 426-444 AND 500-519, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=17827701; DOI=10.1271/bbb.70239;
RA Lee J.-H., Saito S., Mori H., Nishimoto M., Okuyama M., Kim D.,
RA Wongchawalit J., Kimura A., Chiba S.;
RT "Molecular cloning of cDNA for trehalase from the European honeybee, Apis
RT mellifera L., and its heterologous expression in Pichia pastoris.";
RL Biosci. Biotechnol. Biochem. 71:2256-2265(2007).
RN [2] {ECO:0000305}
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND GLYCOSYLATION.
RX PubMed=11826961; DOI=10.1271/bbb.65.2657;
RA Lee J.-H., Tsuji M., Nakamura M., Nishimoto M., Okuyama M., Mori H.,
RA Kimura A., Matsui H., Chiba S.;
RT "Purification and identification of the essential ionizable groups of
RT honeybee, Apis mellifera L., trehalase.";
RL Biosci. Biotechnol. Biochem. 65:2657-2665(2001).
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:0000269|PubMed:11826961, ECO:0000269|PubMed:17827701};
CC -!- ACTIVITY REGULATION: Inhibited by sodium, potassium and ammonium ions,
CC and by TEMED. {ECO:0000269|PubMed:11826961}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.66 mM for alpha,alpha-trehalose (in 0.1 M sodium phosphate pH
CC 6.75, at 35 degrees Celsius) {ECO:0000269|PubMed:11826961,
CC ECO:0000269|PubMed:17827701};
CC KM=0.52 mM for alpha,alpha-trehalose (in 50 mM sodium phosphate pH
CC 6.6, at 35 degrees Celsius) {ECO:0000269|PubMed:11826961,
CC ECO:0000269|PubMed:17827701};
CC pH dependence:
CC Optimum pH is 6.7 when incubated for 5 minutes at 35 degrees Celsius.
CC Active from pH 4.5 to 12.5 when incubated for 5 minutes at 35 degrees
CC Celsius. Optimum pH is 7.0 when incubated for 24 hours at 4 degrees
CC Celsius. Active from pH 5.0 to 10.5 when incubated for 24 hours at 4
CC degrees Celsius. {ECO:0000269|PubMed:11826961,
CC ECO:0000269|PubMed:17827701};
CC Temperature dependence:
CC Stable up to 40 degrees Celsius, but activity is lost after 15
CC minutes incubation at 60 degrees Celsius.
CC {ECO:0000269|PubMed:11826961, ECO:0000269|PubMed:17827701};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11826961}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Glycosylated; contains 3.1% carbohydrates.
CC {ECO:0000269|PubMed:11826961}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000255}.
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; AB301556; BAF81545.1; -; mRNA.
DR RefSeq; NP_001106141.1; NM_001112671.1.
DR AlphaFoldDB; A8J4S9; -.
DR SMR; A8J4S9; -.
DR STRING; 7460.GB55489-PA; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR PaxDb; A8J4S9; -.
DR EnsemblMetazoa; NM_001112671; NP_001106141; LOC410795.
DR GeneID; 410795; -.
DR KEGG; ame:410795; -.
DR eggNOG; KOG0602; Eukaryota.
DR PhylomeDB; A8J4S9; -.
DR BioCyc; MetaCyc:MON-17105; -.
DR BRENDA; 3.2.1.28; 387.
DR Proteomes; UP000005203; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0005991; P:trehalose metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..626
FT /note="Trehalase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000314636"
FT TOPO_DOM 36..595
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 335
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 532
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188..189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 234..236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 299..301
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 626 AA; 72817 MW; 08DAE9FCB49D1426 CRC64;
MASSCSIRCG SRNILVNAAA TFLALLVVLR CFANAEKPSP CQSDVYCRGE LLHTIQMASI
YKDSKTFVDM KMKRPPDETL KSFREFMERH EQMPTRYQIE RFVNDTFDPE GSEFEDWDPD
DWTFRPKFLS RILDDDLRNF ASELNGIWKM LGRKMKDDVR VNEELYSIIY VPHPVIVPGG
RFREFYYWDS YWIVKGLLLS EMYTTVKGML TNFVSLVDKI GFIPNGGRIY YTMRSQPPML
IPMVDEYLKI THDYEWLENN LYLLEKEFDF WMTNRTVEIE VDGVNYVLAR YNEQSSGPRP
ESYKEDYLTS QSFRTNEEKD NYYSELKTAA ESGWDFSSRW FILDGTNKGN LTNLKTRYII
PVDLNSIIYR NAVLLAQYNQ RMGNESKVAY YQKRAAEWKR AIQAVLWHDE VGAWLDYDIL
NDIKRDYFYP TNILPLWTDC YDIAKREEYV SKVLKYLEKN KIMLNLGGIP TTLEHSGEQW
DYPNAWPPLQ YFVIMALNKT EDPWAQRLAY EISERWVRSN YKAYNETHSM FEKYDATVSG
GHGGGGEYEV QLGFGWSNGV IMDLLNRYGD KLTAEDRFVA TFHSNSTPQP VVVSTAGQVM
TGILALVISL AAGFIGKMRC ANNAAQ
