TREA_BOMMO
ID TREA_BOMMO Reviewed; 579 AA.
AC P32358; Q27453;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 16-35; 95-114 AND 289-308.
RC STRAIN=Kinshu X Showa; TISSUE=Pupal midgut;
RX PubMed=7916633; DOI=10.1016/0167-4781(93)90184-f;
RA Su Z.-H., Sato Y., Yamashita O.;
RT "Purification, cDNA cloning and northern blot analysis of trehalase of
RT pupal midgut of the silkworm, Bombyx mori.";
RL Biochim. Biophys. Acta 1173:217-224(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Kinshu X Showa;
RX PubMed=7519445; DOI=10.1016/0167-4781(94)90190-2;
RA Su Z.-H., Ikeda M., Sato Y., Saito H., Imai K., Isobe M., Yamashita O.;
RT "Molecular characterization of ovary trehalase of the silkworm, Bombyx mori
RT and its transcriptional activation by diapause hormone.";
RL Biochim. Biophys. Acta 1218:366-374(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Silk gland;
RA Su Z.-H., Itani Y., Yamashita O.;
RT "Structure of trehalase gene of the silkworm, Bombyx mori and phylogenic
RT relationship of trelalases.";
RL Nihon Sanshigaku Zasshi 66:457-465(1997).
CC -!- FUNCTION: Involved in uptake of hemolymph trehalose into epithelial
CC cells in the midgut of feeding larvae.
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 -!- SUBCELLULAR LOCATION: Basolateral cell membrane.
CC -!- TISSUE SPECIFICITY: In midgut and Malpighian tubules.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR EMBL; D13763; BAA02909.1; -; mRNA.
DR EMBL; S73271; AAC60507.1; -; mRNA.
DR EMBL; D86212; BAA13042.1; -; Genomic_DNA.
DR PIR; S33759; S33759.
DR RefSeq; NP_001037458.1; NM_001043993.1.
DR AlphaFoldDB; P32358; -.
DR SMR; P32358; -.
DR STRING; 7091.BGIBMGA005664-TA; -.
DR BindingDB; P32358; -.
DR ChEMBL; CHEMBL2268008; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR GeneID; 693027; -.
DR KEGG; bmor:693027; -.
DR eggNOG; KOG0602; Eukaryota.
DR HOGENOM; CLU_006451_4_0_1; -.
DR OrthoDB; 417479at2759; -.
DR BRENDA; 3.2.1.28; 890.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
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 Cell membrane; Direct protein sequencing; Glycoprotein; Glycosidase;
KW Hydrolase; Membrane; Reference proteome; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:7916633"
FT CHAIN 16..579
FT /note="Trehalase"
FT /id="PRO_0000012057"
FT REGION 560..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 513
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168..169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214..216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 279..281
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 528
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 30
FT /note="S -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="K -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="K -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="Q -> E (in Ref. 3; BAA13042)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="I -> V (in Ref. 3; BAA13042)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="T -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="A -> T (in Ref. 3; BAA13042)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="F -> L (in Ref. 3; BAA13042)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="V -> I (in Ref. 3; BAA13042)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="V -> I (in Ref. 3; BAA13042)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="A -> E (in Ref. 3; BAA13042)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="E -> K (in Ref. 3; BAA13042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 66542 MW; 263F5D57F9A40297 CRC64;
MRLFLLLVGL TTVIADDLPP TCIRPVYCNS TLLHYVQMAR LYPDSKTFVD FQMRKDENAT
LSAFQELLDR TNHNPTKEDL QEFVVDFFDE TSELEEWKPD DHKENPPFLA KIRDQGFREF
AKALNDIWPT LARRVKPSVL EKPEQSSLVP MTHGFIVPGG RFKEIYYWDA YWIIEGLLIT
DMTETAKGMI ENLIELLYKF GHIPNGSRWY YQERSQPPLL AAMIKLYYEK TKDIEFIRKY
ISALEKELEY WLDTHLIAFN KDDRVYTLLR YYIPSAGPRP ESYYEDYELA QKLDKNTDPN
DIYADLKSAA ESGWDFSTRW FISESGDNSG NLTNLNTKNV IPVDLNAIFA GALQITANFQ
AILKNPRRAA HWGYMAEQWR SSIEQALWDE EDGVWHDYDI LNNKPRRYFY TSNLAPLWMN
AVEKPFLAKH GARVLEYLHE SQALEYPGGV PVSLVNSGEQ WDFPNAWPPE VSIVVTAIQN
IGSEESSKLA KELAQVWVRA CKSGFTEKKQ MFEKYDALNA GKYGGGGEYT VQDGFGWSNG
VVLEFLDRYG AVLTSVDSVD ASANNGQSNE ESETDSKEK
