TREA_CANAX
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 03-AUG-2022, entry version 73.
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; Saccharomycetes;
OC Saccharomycetales; 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 PRIDE; P52494; -.
DR VEuPathDB; FungiDB:CAWG_01415; -.
DR VEuPathDB; FungiDB:CR_00560W_A; -.
DR BRENDA; 3.2.1.28; 1096.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IEA:EnsemblFungi.
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 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.
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 69..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Polar 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
