ID   TRE_ORYSJ               Reviewed;         563 AA.
AC   Q9FWC1; A0A0P0XWC5; Q7XCP2;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable trehalase;
DE            EC=3.2.1.28;
DE   AltName: Full=Alpha,alpha-trehalase;
DE   AltName: Full=Alpha,alpha-trehalose glucohydrolase;
GN   OrderedLocusNames=Os10g0521000, LOC_Os10g37660; ORFNames=OSJNBb0018B10.19;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA   Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA   Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA   Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA   Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA   Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA   Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA   Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA   Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA   Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA   Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA   Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA   Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA   Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA   Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Involved in the regulation of trehalose content by
CC       hydrolyzing trehalose to glucose. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR   EMBL; AC051634; AAG13442.1; -; Genomic_DNA.
DR   EMBL; DP000086; AAP54665.1; -; Genomic_DNA.
DR   EMBL; AP008216; BAF27001.1; -; Genomic_DNA.
DR   EMBL; AP014966; BAT11704.1; -; Genomic_DNA.
DR   EMBL; AK108163; BAG98305.1; -; mRNA.
DR   AlphaFoldDB; Q9FWC1; -.
DR   SMR; Q9FWC1; -.
DR   STRING; 4530.OS10T0521000-01; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   PaxDb; Q9FWC1; -.
DR   PRIDE; Q9FWC1; -.
DR   EnsemblPlants; Os10t0521000-01; Os10t0521000-01; Os10g0521000.
DR   Gramene; Os10t0521000-01; Os10t0521000-01; Os10g0521000.
DR   eggNOG; KOG0602; Eukaryota.
DR   HOGENOM; CLU_006451_4_2_1; -.
DR   InParanoid; Q9FWC1; -.
DR   OMA; TNGVLIW; -.
DR   PlantReactome; R-OSA-1119601; Trehalose degradation II.
DR   Proteomes; UP000000763; Chromosome 10.
DR   Proteomes; UP000059680; Chromosome 10.
DR   Genevisible; Q9FWC1; OS.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IBA:GO_Central.
DR   GO; GO:0005993; P:trehalose catabolic process; IBA:GO_Central.
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; PS00928; TREHALASE_2; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Reference proteome; Stress response.
FT   CHAIN           1..563
FT                   /note="Probable trehalase"
FT                   /id="PRO_0000417664"
FT   ACT_SITE        309
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        517
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207..209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         532
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   563 AA;  62782 MW;  F6457370B7DBD3BF CRC64;
     MAPTAAVAGG GVEAEALLGL LQRVQSEALR AFGPNDFDPK LYVDLPLAAD ASAAAALASL
     PRAAPSRGEM EAYISRYFAL AGSDLVAAAD PPDFERDPPG FLPRVERAEA RAWALEVHAL
     WKDLTRRVAP AVAARPDRHT LLPLPGRVVV PGSRFREVYY WDSYWVVRGL LVSKMYETAK
     DIVLNLVYLV EKYGFVLNGA RSYYTNRSQP PLLSSMVLDI YMATGDMAFV RRVFPSLLKE
     HSFWMSEVHN VAVMDNHGRV HNLSRYQAMW NKPRPESATI DEEFASKLST AAKEKFYHQV
     ASTAETGWDF SSRWMRDSTD MTTLTTSCII PVDLNTFILK MEQDIAFFAK LIGESTTSEI
     FSEASKARHN AIDSVLWNAD MEQWLDYWLP TDGNCQGVYQ WKSISQNRAI FASNFVPLWL
     NAQHSGLEQF VDEAKSVRVM RSLQKSGLLQ PAGIATSLSN TGQQWDFPNG WAPLQHLIVE
     GLLRSGSGEA RELAEDIATR WVRTNYDAYK ATGAMHEKYD VVTCGKSGGG GEYKPQTGFG
     WSNGVILSFL DEFGWPQDKK IDC