ID   TREH_THEAC              Reviewed;         581 AA.
AC   Q9HLE2;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Trehalase {ECO:0000303|PubMed:25979886};
DE            EC=3.2.1.28 {ECO:0000269|PubMed:25979886};
DE   AltName: Full=Alpha,alpha-trehalase {ECO:0000305};
GN   OrderedLocusNames=Ta0286 {ECO:0000312|EMBL:CAC11431.1};
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=25979886; DOI=10.1128/aem.00956-15;
RA   Sakaguchi M., Shimodaira S., Ishida S.N., Amemiya M., Honda S.,
RA   Sugahara Y., Oyama F., Kawakita M.;
RT   "Identification of GH15 family thermophilic archaeal trehalases that
RT   function within a narrow acidic-pH range.";
RL   Appl. Environ. Microbiol. 81:4920-4931(2015).
CC   -!- FUNCTION: Catalyzes the hydrolysis of alpha,alpha-trehalose into two
CC       molecules of D-glucose. {ECO:0000269|PubMed:25979886}.
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:0000269|PubMed:25979886};
CC   -!- ACTIVITY REGULATION: Inhibited by validamycin A.
CC       {ECO:0000269|PubMed:25979886}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=40.2 mM for trehalose {ECO:0000269|PubMed:25979886};
CC         Note=kcat is 66.7 sec(-1). {ECO:0000269|PubMed:25979886};
CC       pH dependence:
CC         Optimum pH is 3.7. Active within a narrow range of acidic pH values
CC         (pH 3.2 to 3.9). {ECO:0000269|PubMed:25979886};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:25979886};
CC   -!- PATHWAY: Glycan degradation; trehalose degradation; D-glucose from
CC       alpha,alpha-trehalose: step 1/1. {ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25979886}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR   EMBL; AL445063; CAC11431.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HLE2; -.
DR   SMR; Q9HLE2; -.
DR   STRING; 273075.Ta0286m; -.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   DNASU; 1456992; -.
DR   EnsemblBacteria; CAC11431; CAC11431; CAC11431.
DR   KEGG; tac:Ta0286; -.
DR   eggNOG; arCOG03286; Archaea.
DR   HOGENOM; CLU_010399_2_0_2; -.
DR   OMA; VEWMCVP; -.
DR   UniPathway; UPA00300; UER00535.
DR   Proteomes; UP000001024; Chromosome.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005993; P:trehalose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR045582; Trehalase-like_N.
DR   Pfam; PF19291; DUF5911; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 2.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..581
FT                   /note="Trehalase"
FT                   /id="PRO_0000448960"
SQ   SEQUENCE   581 AA;  67332 MW;  1ACE44E36D05DED1 CRC64;
     MLVAMNGFID WGCLPNFNSP AVFSSILDKK KGGYFAIYPT DTHDLYVDQY YKELTNILVT
     EFIKNGKVIL RTTDFMPDSE YGKISFPEVH RFVETFSDPV RITIDFKPAF NYATERPLIQ
     RVQHGFIFST EKENMGISTE FQLKKNADHV FADVDMEPRS SSWVIALYGI HHLYRPTDYK
     SYLRLQETTD YWRKWASNST YSGMYHSMVM RSALALKVLF YEPTGMMVAA PTASLPEAIG
     GERNWDYRYT WIRDTAYVIE ALATIGYKRE AVSFLYDMMD VISRENKIRT IYSIDNSDDF
     VERELDFEGY RGSRPVRIGN KAVDQLQIDQ YGSIVRAIHA MEKAGGVVNS YLWDFVEEMM
     AKIEYLWKYP DSSIWEFRTE PKQYVYSKVM SWAAFDSAIT MARDLGLTAP IKKWKGIQDE
     IWNDVMTKGF DPQTNSFVQY YGSKNVDASL LRLPILGFIP ANDERFIGTM KRIEDELMVD
     GYLFRRYRED DGLKGDEGSF LMLTFWYIED LILMKRLKAA RAALESIIEK ANHLGLYSEE
     IDEKTGDFLG NFPQALSHLG IIRVAPKLEE AFLKRVSKIN E