TREA_BEAB2
ID TREA_BEAB2 Reviewed; 743 AA.
AC J5K1E2;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Cytosolic neutral trehalase {ECO:0000305};
DE EC=3.2.1.28 {ECO:0000269|PubMed:20630729};
DE AltName: Full=Alpha,alpha-trehalase {ECO:0000305};
DE AltName: Full=Alpha-trehalose glucohydrolase {ECO:0000255|RuleBase:RU361180};
GN Name=NTH1 {ECO:0000303|PubMed:20630729};
GN ORFNames=BBA_01127 {ECO:0000312|EMBL:EJP70258.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000312|Proteomes:UP000002762};
RN [1] {ECO:0000312|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000312|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y.,
RA St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20630729; DOI=10.1016/j.micres.2010.04.001;
RA Liu Q., Ying S.H., Feng M.G.;
RT "Characterization of Beauveria bassiana neutral trehalase (BbNTH1) and
RT recognition of crucial stress-responsive elements to control its expression
RT in response to multiple stresses.";
RL Microbiol. Res. 166:282-293(2011).
CC -!- FUNCTION: Hydrolyzes intracellular trehalose to glucose.
CC {ECO:0000269|PubMed:20630729}.
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:20630729};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P32356};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0 at 55 degrees Celsius.
CC {ECO:0000269|PubMed:20630729};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius at pH 7.0.
CC {ECO:0000269|PubMed:20630729};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32356}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR EMBL; JH725151; EJP70258.1; -; Genomic_DNA.
DR RefSeq; XP_008594446.1; XM_008596224.1.
DR AlphaFoldDB; J5K1E2; -.
DR SMR; J5K1E2; -.
DR STRING; 655819.J5K1E2; -.
DR EnsemblFungi; BB8028_0003g07070.1; BB8028_0003g07070.1; BB8028_0003g07070.
DR EnsemblFungi; EJP70258; EJP70258; BBA_01127.
DR GeneID; 19884139; -.
DR HOGENOM; CLU_006451_1_1_1; -.
DR InParanoid; J5K1E2; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0015927; F:trehalase activity; IDA:UniProtKB.
DR GO; GO:0005993; P:trehalose catabolic process; IDA: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 InterPro; IPR018232; Glyco_hydro_37_CS.
DR InterPro; IPR011120; Trehalase_Ca-bd.
DR PANTHER; PTHR23403; PTHR23403; 1.
DR Pfam; PF01204; Trehalase; 1.
DR Pfam; PF07492; Trehalase_Ca-bi; 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 Calcium; Cytoplasm; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..743
FT /note="Cytosolic neutral trehalase"
FT /id="PRO_0000452800"
FT ACT_SITE 459
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT ACT_SITE 664
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 292..293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 338..340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 457
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
SQ SEQUENCE 743 AA; 85411 MW; F3D0BB3CA3D42872 CRC64;
MSDSTAPSAH RPRGSEDFGV FDDAKTYYAS DERHTGRFAN RTRTYSQSSL IKQIERLNLP
EPFRRGSHDE SNLEQGRRFL IQVDATLESL KAQEDTDGNM QITIEDSGPK VLPLRTAASA
GYHRFEVRGT YMLSNLLQEL TLAKEYGRKQ IILDEARLNE NPVNRLSRLI KDHFWDGLTR
RIDASSIEIA ARDPKDWTDD PRPRIYIPSK CTAQFEYYKQ VALDRPEIRL DVQLLPEVIT
PEIIRDMNEK PGLLAVAVEE VEEQDPVKGT IKTLRGLPFV VPGGRFNELY GWDSYMESLG
LLVNDRVDLA KAMVLNFCFC IEHYGKILNA TRSYYLGRSQ PPFLTDMALR VYEKIKHEPD
ALEFLRRSIL AAIKEYHSVW TGQARLDPTT GLSRYCPEGL GVPPETEPSH FVHILQPYIK
KHGMEFDEFV RAYNHGEIKE PELDNYFMHD RAVRESGHDT SYRFEGVCAN LATIDLNSLL
FKYETDISRT IRSLFDDKLV MPEEFCQGTP YKPGDILTSA LWDRKAKRRK LTMDKLMWNE
EEGMFFDYDF VNKKRCTYET ATTLWSLWAG LASPKQAADI VKKGLPKFEE FGGLLAGTES
SRGEIGLERP NRQWDYPYGW APQQMLAWTG LLRYSFNEEA ERLAYKWLFM ITKAFVDFNG
VVVEKYDVTR PIDPHRVDAE YGNQGLNFKG VAKEGFGWVN ASYVYGLQIV NAHMRRALGT
LTPYPTFIKA IEQLNEKALA DLE
