TREB_YEAST
ID TREB_YEAST Reviewed; 780 AA.
AC P35172; D6VQ02;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Probable trehalase;
DE EC=3.2.1.28;
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
GN Name=NTH2; OrderedLocusNames=YBR001C; ORFNames=YBR0106;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091860; DOI=10.1002/yea.320100006;
RA Wolfe K.H., Lohan A.J.E.;
RT "Sequence around the centromere of Saccharomyces cerevisiae chromosome II:
RT similarity of CEN2 to CEN4.";
RL Yeast 10:S41-S46(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CHARACTERIZATION.
RX PubMed=7730323; DOI=10.1074/jbc.270.17.10193;
RA Nwaka S., Kopp M., Holzer H.;
RT "Expression and function of the trehalase genes NTH1 and YBR0106 in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:10193-10198(1995).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53 AND SER-112, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 -!- MISCELLANEOUS: Present with 2500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {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; Z26494; CAA81270.1; -; Genomic_DNA.
DR EMBL; Z35870; CAA84937.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07122.1; -; Genomic_DNA.
DR PIR; S44560; S44560.
DR RefSeq; NP_009555.1; NM_001178349.1.
DR AlphaFoldDB; P35172; -.
DR SMR; P35172; -.
DR BioGRID; 32702; 75.
DR DIP; DIP-6841N; -.
DR IntAct; P35172; 3.
DR MINT; P35172; -.
DR STRING; 4932.YBR001C; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR iPTMnet; P35172; -.
DR MaxQB; P35172; -.
DR PaxDb; P35172; -.
DR PRIDE; P35172; -.
DR EnsemblFungi; YBR001C_mRNA; YBR001C; YBR001C.
DR GeneID; 852286; -.
DR KEGG; sce:YBR001C; -.
DR SGD; S000000205; NTH2.
DR VEuPathDB; FungiDB:YBR001C; -.
DR eggNOG; KOG0602; Eukaryota.
DR GeneTree; ENSGT00390000006949; -.
DR HOGENOM; CLU_006451_1_1_1; -.
DR InParanoid; P35172; -.
DR OMA; ERENKEW; -.
DR BioCyc; MetaCyc:YBR001C-MON; -.
DR BioCyc; YEAST:YBR001C-MON; -.
DR PRO; PR:P35172; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P35172; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IMP:SGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005993; P:trehalose catabolic process; IMP:SGD.
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 Glycosidase; Hydrolase; Phosphoprotein; Reference proteome.
FT CHAIN 1..780
FT /note="Probable trehalase"
FT /id="PRO_0000173800"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 507
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 703
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 338..339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 384..386
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 780 AA; 89679 MW; B034B14A68B38C53 CRC64;
MVDFLPKVTE INPPSEGNDG EDNIKPLSSG SEQRPLKEEG QQGGRRHHRR LSSMHEYFDP
FSNAEVYYGP ITDPRKQSKI HRLNRTRTMS VFNKVSDFKN GMKDYTLKRR GSEDDSFLSS
QGNRRFYIDN VDLALDELLA SEDTDKNHQI TIEDTGPKVI KVGTANSNGF KHVNVRGTYM
LSNLLQELTI AKSFGRHQIF LDEARINENP VDRLSRLITT QFWTSLTRRV DLYNIAEIAR
DSKIDTPGAK NPRIYVPYNC PEQYEFYIQA SQMNPSLKLE VEYLPKDITA EYVKSLNDTP
GLLALAMEEH VNPSTGERSL VGYPYAVPGG RFNELYGWDS YLMALGLIES NKVDVARGMV
EHFIFEIDHY SKILNANRSY YLCRSQPPFL TDMALLVFEK IGGKNNPNAI QLLKRAFRAA
IKEYKEVWMS SPRLDSLTGL SCYHSDGIGI PPETEPDHFD TILLPYAEKY NVTLEKLRYL
YNEGMIKEPK LDAFFLHDRA VRESGHDTTY RFEGVCAYLA TIDLNSLLYK YEKDIAFVIK
EYFGNEYKDE NDGTVTDSEH WEELAELRKT RINKYMWDED SGFFFYYNTK LKCRTSYESA
TTFWSLWAGL ATEEQAKITV EKALPQLEML GGLVACTEKS RGPISIDRPI RQWDYPFGWA
PHQILAWKGL SAYGYQQVAT RLAYRWLYMI TKSFVDYNGM VVEKYDVTRG TDPHRVDAEY
GNQGADFKGV ATEGFGWVNT SYLLGLKYMN NHARRALAAC SPPLPFFNSL KPSEKKLYYL
