TREA_DICDI
ID TREA_DICDI Reviewed; 594 AA.
AC Q54QZ5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Trehalase {ECO:0000305};
DE EC=3.2.1.28 {ECO:0000250|UniProtKB:O43280};
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE Flags: Precursor;
GN Name=treh; ORFNames=DDB_G0283473;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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:0000250|UniProtKB:O43280};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR EMBL; AAFI02000055; EAL65721.1; -; Genomic_DNA.
DR RefSeq; XP_639096.1; XM_634004.1.
DR AlphaFoldDB; Q54QZ5; -.
DR SMR; Q54QZ5; -.
DR STRING; 44689.DDB0185541; -.
DR PaxDb; Q54QZ5; -.
DR EnsemblProtists; EAL65721; EAL65721; DDB_G0283473.
DR GeneID; 8624120; -.
DR KEGG; ddi:DDB_G0283473; -.
DR dictyBase; DDB_G0283473; treh.
DR eggNOG; KOG0602; Eukaryota.
DR HOGENOM; CLU_006451_4_0_1; -.
DR InParanoid; Q54QZ5; -.
DR OMA; TNGVLIW; -.
DR PhylomeDB; Q54QZ5; -.
DR PRO; PR:Q54QZ5; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; ISS:UniProtKB.
DR GO; GO:0005993; P:trehalose catabolic process; ISS:UniProtKB.
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 PANTHER; PTHR23403; PTHR23403; 1.
DR Pfam; PF01204; Trehalase; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..594
FT /note="Trehalase"
FT /id="PRO_0000340239"
FT ACT_SITE 348
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT ACT_SITE 549
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 197..198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 243..245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 312..314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 564
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 594 AA; 67319 MW; B412BDE54F269E57 CRC64;
MDFLNKKIQK ILFICILSFL IVNLTKSEIS EVKDVSKFLS VGGGGTGGCQ HPIYCNGTLL
KTIQLTQVFN DSKTFVDMPM RTSIENVNEL FNQLLLNTSK NGGPNKEELA AFLSENFYPA
GYEVEPVTPV DWVPNPSFLD EITDPNLVDF ARSIHGKWLE LTRVFNTSGL CDGCYSSIPV
NNPFVIAGSR FREFYYWDSY WIIQGLLVSD MTTTAKGMLR NFGDMITEFG FIPNGGRIYY
LNRSQPPLFT QMVNKYFEAT NGSDIEFLQE ILPILDQEYQ WWMTHRTTEL TNGETGESVI
LNLYNVSNNS PRPESYYEDF TDAQSFSSVE EKDYFYSSIA SGAESGWDFS SRWMSPSDNT
NLTTIQTVDV VPVDLNSILY LNEKILSSFH RTLGNNSMAV YYQAQSESRV DAMQQVFFNE
DTYQWNDYNL KTSTNNEAWY TSNILPLFAD IQSSIDMDNQ EIDLIFKSLA NVLIAYPGGV
PTSLISAQSL QWDGLNVWPP LQYWIIESIM TPNTTFSNMI GKNLIDRWIT TNFCGWNSTL
ESEGGMMFEK YNANYIGVPG GGGEYVVQNG FGWTNGVDLY LLKKYGKSIT LNSC
