TREB_ASHGO
ID TREB_ASHGO Reviewed; 738 AA.
AC Q757L1; Q8J1F6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=AER001C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 246-738.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RA Wendland J., Dietrich F.S., Mohr C., Philippsen P.;
RT "Isolation and functional analysis of centromeric DNA of the filamentous
RT ascomycete Ashbya gossypii.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
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DR EMBL; AE016818; AAS52685.1; -; Genomic_DNA.
DR EMBL; AF384989; AAO15410.1; -; Genomic_DNA.
DR RefSeq; NP_984861.1; NM_210215.1.
DR AlphaFoldDB; Q757L1; -.
DR SMR; Q757L1; -.
DR STRING; 33169.AAS52685; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR EnsemblFungi; AAS52685; AAS52685; AGOS_AER001C.
DR GeneID; 4621060; -.
DR KEGG; ago:AGOS_AER001C; -.
DR eggNOG; KOG0602; Eukaryota.
DR HOGENOM; CLU_006451_1_1_1; -.
DR InParanoid; Q757L1; -.
DR OMA; GLERPNR; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IEA:EnsemblFungi.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:EnsemblFungi.
DR GO; GO:0030437; P:ascospore formation; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..738
FT /note="Probable trehalase"
FT /id="PRO_0000173799"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 465
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 660
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 296..297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 342..344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 738 AA; 84487 MW; 16DA18085F1700C7 CRC64;
MLQGMPKRSG SISELHDPFS SPDVYYGPAT DPRRQKQPNK YSRTRTMSII ENVSTFKSAG
KQYNIRRRGS EDDSMLASSG HRKFYIKDVD KTLEELLESE DTDGNYQITI EDRGPKTLRV
GTANSNGFRH VQIRGTYMLS NLLQELTIAK NFGRKQVILD EARLNEDPVN RLTRLITHQF
WDSLTRRIDY NSIAAIAADT KVDTPGAKVP RIYVPHGCPE QYEYFIECSQ LNPSLNLEVK
YLPDVITPEH VQSLNESPGL LALAMESHRD PITGESTLVG FPYVVPGGRF NELYGWDSYL
MALGLLDCNK VDIARGMVEH FIFEIEHYGK ILNANRSYYL CRSQPPFLTD MALKVFEKFG
GDQNPTAVDF LKRAFIAAIK EYKSVWMAEP RYDKTTGLSC YHPDGIGFPP ETEPDHFDAI
CRKFAEKHNV TIPEFRCMYD AGEVHEPELD EFFLHDRAVR ESGHDTSYRL ENVCAYLATI
DLNSLLYKYE KDIAYVVSKY FDDSITDYAG ETTTSSHWEA LADIRKQRIT KYLWDEETGF
FYDYNVHIGK RTSYDSATTF WAMWAGLATQ EQANAMVEKA LPRLEMLGGL VACTEESRGE
ITMNRPSRQW DYPYGWAPHQ MLAWTGLDNY GFTGVARRLA YRWLFLMTKA FVDYNGIVVE
KYDVTRGTDP HRVDAEYGNQ GADFKGVATE GFGWVNSSYI LGLKFMNTYA KRALANCTVP
DIFFKHMKPE EKARYALI
