TREB_NEUCR
ID TREB_NEUCR Reviewed; 744 AA.
AC O42783; Q1K6U9; Q8NIK6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 126.
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=treB {ECO:0000303|PubMed:10320571}; ORFNames=G15D1.050, NCU04221;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=10320571; DOI=10.1046/j.1365-2958.1999.01327.x;
RA d'Enfert C., Bonini B.M., Zapella P.D.A., Fontaine T., da Silva A.M.,
RA Terenzi H.F.;
RT "Neutral trehalases catalyse intracellular trehalose breakdown in the
RT filamentous fungi Aspergillus nidulans and Neurospora crassa.";
RL Mol. Microbiol. 32:471-483(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Hydrolyzes intracellular trehalose to glucose.
CC {ECO:0000250|UniProtKB:P32356}.
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 -!- DEVELOPMENTAL STAGE: Induced during conidial germination.
CC {ECO:0000269|PubMed:10320571}.
CC -!- INDUCTION: Induced during recovery from thermal stress.
CC {ECO:0000269|PubMed:10320571}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC01744.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF044218; AAC01744.1; ALT_FRAME; mRNA.
DR EMBL; AL807369; CAD36994.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA31609.1; -; Genomic_DNA.
DR RefSeq; XP_960845.1; XM_955752.3.
DR AlphaFoldDB; O42783; -.
DR SMR; O42783; -.
DR STRING; 5141.EFNCRP00000003938; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR EnsemblFungi; EAA31609; EAA31609; NCU04221.
DR GeneID; 3876992; -.
DR KEGG; ncr:NCU04221; -.
DR VEuPathDB; FungiDB:NCU04221; -.
DR HOGENOM; CLU_006451_1_1_1; -.
DR InParanoid; O42783; -.
DR OMA; GLERPNR; -.
DR BRENDA; 3.2.1.28; 3627.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 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.
FT CHAIN 1..744
FT /note="Cytosolic neutral trehalase"
FT /id="PRO_0000173796"
FT ACT_SITE 460
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT ACT_SITE 665
FT /note="Proton donor/acceptor"
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 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 293..294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 339..341
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 406
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
SQ SEQUENCE 744 AA; 85969 MW; 0B916903C0656092 CRC64;
MTSQPSSGKG RGRNLSIDEY NVYDDAKTYY TTEDRHHNHR AGARTRTYSQ NSLFKQFERL
GLQKEPYRRG SHDESTIPQS RRFLIQVEPT LQSLQSQEDT DGNMQITIED NGPKVLSLRT
AASNGYNRFD IRGTYMLSNL LQELYLAKEY GRKQIILDEA RLNENPVNRL SRLIKDHFWE
GLTRRIDASS IEIAARDPKD WTDDPRPRIY IPRGAPEQHE YYTKVALDRP ELRLDVQYLP
EKITPEIVRD MNAKPGLLAV DMEEVVDPKT GEKTLRGRPF VVPGGRFNEL YGWDSYMESL
GLLVNDRVDL AKSMVQNFCF CIKHYGKILN ATRSYYLCRS QPPFLTDMTL RVYDKIKHEP
GALEFLRQSL LAAIKEYYSV WTAEPRLDPV TGLSRYRPEG LGVPPETEAG HFIHILEPYA
KKHNMSFDEF VYAYNHGEIK EPTLDDYFMH DRAVRESGHD TTYRFEGICA DLATIDLNSL
LFKYETDIAR TIRNVFHDKF EVPDDWLATN NPAASKLETS AMWDRRAKRR KLAIDKYLWN
EEAGMYFDYN TATRKQCNYE SATTFWALWA GVSNPKQAAA MVTKALPKLE AFGGLLSGTK
ESRGEIGLER PNRQWDYPYG WAPQQILAWT GLYRYGFNEE AERLAYKWLF MITKAFVDFN
GVVVEKYDVT RPIDPHRVDA EYGNQGLDFK GVAKEGFGWV NASYVYGLQI VNAHMRRALG
TLTPYETFMK AVEENRNKAL SELV
