ID A7XZC0_SPOEX Unreviewed; 645 AA.
AC A7XZC0;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Trehalase {ECO:0000256|ARBA:ARBA00019905, ECO:0000256|RuleBase:RU361180};
DE EC=3.2.1.28 {ECO:0000256|ARBA:ARBA00012757, ECO:0000256|RuleBase:RU361180};
DE AltName: Full=Alpha-trehalose glucohydrolase {ECO:0000256|RuleBase:RU361180};
OS Spodoptera exigua (Beet armyworm) (Noctua fulgens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=7107 {ECO:0000313|EMBL:ABU95354.1};
RN [1] {ECO:0000313|EMBL:ABU95354.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18492231; DOI=10.1186/1471-2199-9-51;
RA Tang B., Chen X., Liu Y., Tian H., Liu J., Hu J., Xu W., Zhang W.;
RT "Characterization and expression patterns of a membrane-bound trehalase
RT from Spodoptera exigua.";
RL BMC Mol. Biol. 9:51-51(2008).
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|ARBA:ARBA00001576,
CC ECO:0000256|RuleBase:RU361180};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family.
CC {ECO:0000256|ARBA:ARBA00005615, ECO:0000256|RuleBase:RU361180}.
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; EU106080; ABU95354.1; -; mRNA.
DR AlphaFoldDB; A7XZC0; -.
DR SMR; A7XZC0; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR BRENDA; 3.2.1.28; 5835.
DR GO; GO:0016020; C: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; TREHALASE; 1.
DR PANTHER; PTHR23403:SF1; 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 2: Evidence at transcript level;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361180};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..645
FT /note="Trehalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002717520"
FT TRANSMEM 586..607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 645 AA; 73883 MW; 75678074C09F1846 CRC64;
MYKKMWCVFI AILGVAAGMD RSHLPPTCSS NIYCHGPLLD TVQMAGLYND SKTFVDMKLK
LSANITMDHF HEMMARTGSH PTKADIQEFV NQNFDPEGSE FEDWRPTDWK DNPAFLQNIK
DPLLHEWAAD LNRLWLQLGR KMKPDVKENQ DLYSIIYVDN PVIVPGGRFR EFYYWDSYWI
IKGLLLSEMR STARGMVSNF MDIVERIGFI PNGGRIYYAM RSQPPLLIPM VKLILDDMDD
IEFLRQHIHT LDREYDYWMT NHTVEVHHNG HRYTLARYFD QSQGPRPESY KEDVDVARHF
DTNDKKEELY AELKAAAESG WDFSSRWFIL NGTNKGNLTN LKTRSIIPVD LNAIMCWNAQ
LLRDFHTRLG NVDKAEYYRN VHARFMDAIE QVLWHEDVGV WLDYSLESGR RRDYFYPSNV
SPLWAVCYDQ ARKDYYVNRV VNYLDKVKVD IFDGGIPTTF EHSGEQWDYP NAWPPLQYIV
VMGLANTGQP EAVRLASEIA TKWVRSNFEV WKQKTAMLEK YDATIFGGLG GGGEYVVQTG
FGWTNGVIMA MLNRWGDTTT SADAFGTGAA ADSGAVYGAH VGASGVATAI LVVLASLAAG
TLGLMVYRKR KDYIRVSGGE DYKLLSRKPY TELRSLNGAS NPRQR
//
