ID   TREA_CANAX              Reviewed;         907 AA.
AC   P52494;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=Cytosolic neutral trehalase {ECO:0000303|PubMed:9421900};
DE            EC=3.2.1.28 {ECO:0000305|PubMed:9421900};
DE   AltName: Full=Alpha,alpha-trehalase;
DE   AltName: Full=Alpha,alpha-trehalose glucohydrolase;
GN   Name=NTC1 {ECO:0000303|PubMed:9421900};
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   ACTIVITY REGULATION.
RC   STRAIN=3153A, and Rueck;
RX   PubMed=9421900; DOI=10.1099/00221287-143-12-3747;
RA   Eck R., Bergmann C., Ziegelbauer K., Schoenfeld W., Kuenkel W.;
RT   "A neutral trehalase gene from Candida albicans: molecular cloning,
RT   characterization and disruption.";
RL   Microbiology 143:3747-3756(1997).
CC   -!- FUNCTION: Hydrolyzes intracellular trehalose to glucose.
CC       {ECO:0000305|PubMed:9421900}.
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:9421900};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P32356};
CC   -!- ACTIVITY REGULATION: Inhibited by validamycin A.
CC       {ECO:0000305|PubMed:9421900}.
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; X95099; CAA64476.1; -; Genomic_DNA.
DR   AlphaFoldDB; P52494; -.
DR   SMR; P52494; -.
DR   CAZy; GH37; Glycoside Hydrolase Family 37.
DR   EnsemblFungi; CR_00560W_A-T; CR_00560W_A-T-p1; CR_00560W_A.
DR   VEuPathDB; FungiDB:CAWG_01415; -.
DR   VEuPathDB; FungiDB:CR_00560W_A; -.
DR   BRENDA; 3.2.1.28; 1096.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
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; IEA:EnsemblFungi.
DR   FunFam; 1.50.10.10:FF:000026; Trehalase; 1.
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:SF6; CYTOSOLIC NEUTRAL TREHALASE-RELATED; 1.
DR   PANTHER; PTHR23403; TREHALASE; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   Pfam; PF07492; Trehalase_Ca-bi; 1.
DR   PRINTS; PR00744; GLHYDRLASE37.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 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.
FT   CHAIN           1..907
FT                   /note="Cytosolic neutral trehalase"
FT                   /id="PRO_0000173792"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          39..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..91
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..120
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        631
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   ACT_SITE        831
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   BINDING         242
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   BINDING         244
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   BINDING         246
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   BINDING         248
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   BINDING         253
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   BINDING         439
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P13482"
FT   BINDING         446..447
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   BINDING         495
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   BINDING         504..506
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   BINDING         576
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   BINDING         626
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   BINDING         629
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32356"
FT   VARIANT         687
FT                   /note="K -> N (in strain: 3153A)"
SQ   SEQUENCE   907 AA;  104023 MW;  6B21D4CCD900C793 CRC64;
     MFTKNHRRMS STSSDDDPFD VAEKYYGEER KKKLNRVRTF SAFESTKYGA GPISPLRPTY
     EPPPVIKETS EPLSSSSSTS SPPTLTPQTS QVQFNLGVGK TKNGSAIHSD SEEEEEDEDP
     VSNTKKGEAD EKDPFDTTDS KLENENSTPS SITGKEIIPH PTGFRGSSEE SAIRRKPSII
     PIYHDNISQE SVIRNANTPT TYNREKFHLR RGSLDESTFI RPKKYYINDV QGTLRELLAN
     EDTDNNCQIT IEDTGPKVLR LGTANSLGIN QSSIRGTYRL SNLLQELTIA SRFGRHQIVL
     DEARLSENPV DRMKRLISTS FWNNLTRIIT KENIVDMAKD TKIKESWIDD QGKLHENQES
     HRIYVPYNRK DQYEFFQLIK KQRSDIQLDV QYLPQKIDAD YIKSINKKPG LLSIATRPDP
     QAPDSGSLIS WPYVVPGGRF NELYGWDSYM ETLGLLTDVK IDPSGNPRNL RHLELARGMA
     ENFIYEIHHY GKILNANRSY YLGRSQPPFL TDMALRIFNK TIEVTPELMD EAIDFLKRAT
     LAAIKEYETI WCAHPRLDDK TGLSCYHPEG KGIPPETEPT HFNALLKPYL AKYNDIDQLD
     FIEKYNSGEI KEPELDEYFL HDRAVRESGH DTSYRLEGKC AYLATVDLNS LLYKYENDIA
     FILQSFFNDN LQDPYDDNNS NKIHSSKIWL ERSHQRKLNV DKYLWNEQDG IYYDYNVKLQ
     QQTNYESATT FWPLYAKLAS SNQAAKLIDQ SLHKFEEHGG LVAGTLKSRG EVGLTRPSRQ
     WDYPFGWAPQ QILAWIGLVN YGYDGIARRL AYRWLFMMTK SFVDYNGVIV EKYNVTKGAV
     PHRVDAEYGN QGLDFKGVAT EGFGWVNASY VFGLTFLNLY AQRALGSLTP PEIFLRNMHP
     EQRKQYK
//