TREA_KLULA
ID TREA_KLULA Reviewed; 754 AA.
AC P49381;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Cytosolic neutral trehalase {ECO:0000303|PubMed:9075620};
DE EC=3.2.1.28 {ECO:0000305|PubMed:9075620};
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE AltName: Full=KlNTH1 {ECO:0000303|PubMed:9075620};
GN Name=NTH1 {ECO:0000303|PubMed:9075620}; OrderedLocusNames=KLLA0E17325g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=9075620; DOI=10.1007/s002030050436;
RA Amaral F.C., van Dijck P., Nicoli J.R., Thevelein J.M.;
RT "Molecular cloning of the neutral trehalase gene from Kluyveromyces lactis
RT and the distinction between neutral and acid trehalases.";
RL Arch. Microbiol. 167:202-208(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Hydrolyzes intracellular trehalose to glucose (Probable). The
CC disaccharide trehalose serves as a storage molecule for energy and
CC carbohydrates that is mobilized during nutrient stress
CC (PubMed:9075620). {ECO:0000269|PubMed:9075620,
CC ECO:0000305|PubMed:9075620}.
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:9075620};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000305|PubMed:9075620};
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; X81421; CAA57181.1; -; Genomic_DNA.
DR EMBL; CR382125; CAG99815.1; -; Genomic_DNA.
DR RefSeq; XP_454728.1; XM_454728.1.
DR AlphaFoldDB; P49381; -.
DR SMR; P49381; -.
DR STRING; 28985.XP_454728.1; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR PRIDE; P49381; -.
DR EnsemblFungi; CAG99815; CAG99815; KLLA0_E17271g.
DR GeneID; 2894277; -.
DR KEGG; kla:KLLA0_E17271g; -.
DR eggNOG; KOG0602; Eukaryota.
DR HOGENOM; CLU_006451_1_1_1; -.
DR InParanoid; P49381; -.
DR OMA; GLERPNR; -.
DR Proteomes; UP000000598; Chromosome E.
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 1: Evidence at protein level;
KW Calcium; Cytoplasm; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..754
FT /note="Cytosolic neutral trehalase"
FT /id="PRO_0000173794"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 481
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT ACT_SITE 676
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 312..313
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 358..360
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 476
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
SQ SEQUENCE 754 AA; 86920 MW; 654C9083C52A879D CRC64;
MDGKVNNNPP RSRHRRTSSL EEVVDPFSTP DVYYGPKSDP SKLLSKNRFT RTRTFSVAEP
GGGKGHSSSY TSPYFDTTVP LRRRGSEDDS YSASQGQRRF YIEDVDKTLK ELLASEDTDG
NYQITIEDTG PKVIRVGTVN SNGYKHVHIR GTYMLSNLLQ ELTLAKLFNR KQVILDEARL
NENPVNRMTR LISGQFWKSL TRRIDSNNIA KIAYDTKIDT PKAKNPRIYV PYNCQDEYQQ
LVQWSEMDPS LQLEVNYLPK DITPEFVKSL NDKPGLLCLA MESHMDPVTG EETWVGFPYA
VPGGRFNELY GWDSYFMALG LLESNKLDVA RGMVEHFIFE IDHYGKILNA NRSYYLCRSQ
PPFLTDMALQ VCRKMGGDKN PVAVDLLRRA FKAAIKEYLT VWTASPRLDE KTGLSCYHPD
GIGIPPETEP GHFDSILRKY AEKYNVSIPE FRDLYNSQKV HEPDLDVFFL HDRGVRESGH
DTTYRFENVC AYLATIDLNS LLYKYEVDIA YVIKKYFGDN FEGLPEGHRT SNDWEKLAEV
RKERIDKYLW DEETGFYYDY NVKTEKRTSY ESVTTFWALW AGMSSQEQAQ RMVENALPKL
EEFGGLVACT ARSRGELSLD RPTRQWDYPF GWAPHQILVW DGLVRYGYEN HTRRLAYRWL
FLMTKAFVDY NGIVVEKYDV TRGTDPHRVD AEYGNQGADF KGVATEGFGW VNSSYLLGMK
YMNNFARRAL GTCVTPKVFF GRLPPKEKKK YGLE
