TREA_BOTFB
ID TREA_BOTFB Reviewed; 727 AA.
AC A0A384JRP0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Cytosolic neutral trehalase {ECO:0000305};
DE EC=3.2.1.28 {ECO:0000305|PubMed:16946258};
DE AltName: Full=Alpha,alpha-trehalase {ECO:0000305};
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase {ECO:0000305};
DE AltName: Full=Bctre1 {ECO:0000303|PubMed:16946258};
GN Name=TRE1 {ECO:0000303|PubMed:16946258};
GN ORFNames=BCIN_09g01310 {ECO:0000312|EMBL:ATZ53256.1};
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648 {ECO:0000312|Proteomes:UP000001798};
RN [1] {ECO:0000312|Proteomes:UP000001798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10 {ECO:0000312|Proteomes:UP000001798};
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
RN [2] {ECO:0000312|Proteomes:UP000001798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10 {ECO:0000312|Proteomes:UP000001798};
RX PubMed=23104368; DOI=10.1128/ec.00164-12;
RA Staats M., van Kan J.A.L.;
RT "Genome update of Botrytis cinerea strains B05.10 and T4.";
RL Eukaryot. Cell 11:1413-1414(2012).
RN [3] {ECO:0000312|Proteomes:UP000001798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10 {ECO:0000312|Proteomes:UP000001798};
RX PubMed=26913498; DOI=10.1111/mpp.12384;
RA van Kan J.A.L., Stassen J.H.M., Mosbach A., van der Lee T.A.J., Faino L.,
RA Farmer A.D., Papasotiriou D.G., Zhou S., Seidl M.F., Cottam E., Edel D.,
RA Hahn M., Schwartz D.C., Dietrich R.A., Widdison S., Scalliet G.;
RT "A gapless genome sequence of the fungus Botrytis cinerea.";
RL Mol. Plant Pathol. 18:75-89(2017).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16946258; DOI=10.1099/mic.0.29044-0;
RA Doehlemann G., Berndt P., Hahn M.;
RT "Trehalose metabolism is important for heat stress tolerance and spore
RT germination of Botrytis cinerea.";
RL Microbiology 152:2625-2634(2006).
CC -!- FUNCTION: Hydrolyzes intracellular trehalose to glucose
CC (PubMed:16946258). The disaccharide trehalose serves as a storage
CC carbohydrate that is mobilized during conidial germination
CC (PubMed:16946258). Regulates the level of trehalose as a protectant for
CC cell integrity (PubMed:16946258). {ECO:0000269|PubMed:16946258}.
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:0000305|PubMed:16946258};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P32356};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000305|PubMed:16946258}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32356}.
CC -!- DISRUPTION PHENOTYPE: Increases cellular trehalose levels
CC (PubMed:16946258). Decreases conidial germination frequency
CC (PubMed:16946258). Resistance to thermal stress (PubMed:16946258).
CC {ECO:0000269|PubMed:16946258}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR EMBL; CP009813; ATZ53256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A384JRP0; -.
DR SMR; A0A384JRP0; -.
DR VEuPathDB; FungiDB:Bcin09g01310; -.
DR Proteomes; UP000001798; Chromosome bcin09.
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:0005993; P:trehalose catabolic 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 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 3: Inferred from homology;
KW Calcium; Cytoplasm; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..727
FT /note="Cytosolic neutral trehalase"
FT /id="PRO_0000452801"
FT REGION 47..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 454
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT ACT_SITE 658
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 287..288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 333..335
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 452
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
SQ SEQUENCE 727 AA; 83085 MW; DB3F46A4F84C92B8 CRC64;
MTSPLRKHRT SSVSSEIDPF AAAHVYYSND TNQKSFRQAR TRTYSSNQGI FSTPISGLEK
PKRRGSHDDI GDHGRKFLIQ VDSTLEALRK QEDTDDNHQI TIEDVGPKSL PLGTATSNGF
RRYDIRGTYM LSNLLQELTL AKENGREQII LDESRLNENP VNRLSRLIQG SFWDGLTRRI
DGSVIEIAGR DPKDWTDDPR PRIYIPRGAP EQHAYYTKVA TDRPEVRLDV CWLPEKITPE
VVRDMNSKPG LLAVAMEEVI DPSTGEKTLK GLPFVVPGGR FNELYGWDSY MESLGLIVND
KVHLAKSMVQ NFCFCIEHYG KILNATRSYY LCRSQPPFLT DMALRVFDKI KHEPGSLDFL
KTAILAAIKE YHSVWTAEPR YDPVTGLSRY RPEGLGVPPE TEASHFEHLL APYAEKYNMT
FKEFVDAYNN GRVVEKELDD YFLHDRAVRE SGHDTSYRLE RVCADLATID LNSLLYKYEK
DIAYTIRTFF QDKLEVPAEF CVGDMTPGQL QTSSMWDRRA RGRKLAIDKY LWNKEKGMYF
DYNTLKKEQC TYESATTFWA MWAGVASPQQ AASLVTNALP KFEAAGGLLS GTEESRGAVG
LDRPNRQWDY PYGWAPQQML AWTGLLRYNY QEDAERLAYK WLFMITTAFV DFNGVVVEKY
DVTRVVDPHK VDAEYGNQGS DFKGVAKEGF GWVNASYVYG LQIINAHMRR TLGTLTPWDQ
YNKAMNL
