TREB_MAGO7
ID TREB_MAGO7 Reviewed; 736 AA.
AC O42622; G4N1V8; Q875L8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cytosolic neutral trehalase;
DE EC=3.2.1.28 {ECO:0000250|UniProtKB:P32356};
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
GN Name=NTH1; Synonyms=PTH9; ORFNames=MGG_09471;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=4091-5-8;
RX PubMed=9574508; DOI=10.1094/mpmi.1998.11.5.404;
RA Sweigard J.A., Carroll A.M., Farrall L.F., Chumley F.G., Valent B.;
RT "Magnaporthe grisea pathogenicity genes obtained through insertional
RT mutagenesis.";
RL Mol. Plant Microbe Interact. 11:404-412(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND FUNCTION.
RC STRAIN=Guyane 11;
RX PubMed=12514128; DOI=10.1093/emboj/cdg018;
RA Foster A.J., Jenkinson J.M., Talbot N.J.;
RT "Trehalose synthesis and metabolism are required at different stages of
RT plant infection by Magnaporthe grisea.";
RL EMBO J. 22:225-235(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- FUNCTION: Hydrolyzes intracellular trehalose to glucose (By
CC similarity). Plays a role in pathogenicity, specifically in
CC proliferation of invasive hyphae in rice blast disease
CC (PubMed:12514128). {ECO:0000250|UniProtKB:P32356,
CC ECO:0000269|PubMed:12514128}.
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:P32356};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P32356};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32356}.
CC -!- INDUCTION: During sporulation, plant infection and in response to
CC hyperosmotic stress. {ECO:0000269|PubMed:12514128}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR EMBL; AF027981; AAB88889.1; -; Genomic_DNA.
DR EMBL; AY148092; AAN46743.1; -; Genomic_DNA.
DR EMBL; CM001233; EHA52473.1; -; Genomic_DNA.
DR RefSeq; XP_003712280.1; XM_003712232.1.
DR AlphaFoldDB; O42622; -.
DR SMR; O42622; -.
DR STRING; 318829.MGG_09471T0; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR EnsemblFungi; MGG_09471T0; MGG_09471T0; MGG_09471.
DR GeneID; 2680514; -.
DR KEGG; mgr:MGG_09471; -.
DR VEuPathDB; FungiDB:MGG_09471; -.
DR eggNOG; KOG0602; Eukaryota.
DR HOGENOM; CLU_006451_1_1_1; -.
DR InParanoid; O42622; -.
DR OMA; GLERPNR; -.
DR OrthoDB; 417479at2759; -.
DR PHI-base; PHI:123; -.
DR PHI-base; PHI:7227; -.
DR PHI-base; PHI:775; -.
DR PHI-base; PHI:794; -.
DR Proteomes; UP000009058; Chromosome 3.
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 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..736
FT /note="Cytosolic neutral trehalase"
FT /id="PRO_0000173795"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 453
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT ACT_SITE 657
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 286..287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 332..334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 451
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT VARIANT 394
FT /note="T -> A (in strain: Guyane 11)"
SQ SEQUENCE 736 AA; 84603 MW; 6F8CDE4C8CAB0983 CRC64;
MSEAPQARRV GSVDDHSVYD DAKTYYTSEE RHNNSRSGPR QRTYSQNSLL GQMERLGLKE
PFRRGSHDES NHNRRFLIQV DPTLESLKSQ EDTDGNMQIT IEDNGPKVLT LRTAGSNGHN
RFDIRGTYML SNLLQELTLA QEYGRKQVIL DEARLNENPV NRLSRLIRDH FWDALTRRID
ASSIEVAAKD PKDWTDDPRP RIYVPKGAPE QLEYYKKLAA DKPDIRLDVV ELPETITPEY
VVGINKAPGL LAVDMEETVD PKTGERVMSG RPFVVPGGRF NELYGWDSYM ESLGLLVNDK
VYLAKSMVLN FCFCIKHYGK ILNATRSYYL CRSQPPFLTD MALRVYDKIR HEPDATEFLR
TAILAAIKEY HSVWVAEPRL DPVTGLSRYR PEGTGVPPET EADHFLHILE PYYKKHNMTF
KEFVEAYNFG RIREPELDKY FLHDRAVRES GHDTSYRLEG VCADLATVDL NTLLFKYETD
IARTIRNVFG DKLVIPAEYC VGSLQPGQVE TSAIWDRRSK RRKLAIDKYL WNEEAGMYFD
YDTAKRQQCN YESCTTFWAL WAGVASPKQA AIMVTRALPK FEAYGGLLSG TEESRGQIGL
DRPNRQWDYP YGWAPQQMLA WTGLYRYSFT EEAERLAYKW LFMITKAFSD FNGVVVEKYD
VTRPVDPHRV DAEYGNQGLG FKGVAKEGFG WVNASYIYGL QIINAHMRRA LGTLTPYDTF
IKALEDNRNR ALSEMV
