ID   TREH_THEVO              Reviewed;         623 AA.
AC   Q978S7;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   04-NOV-2026, entry version 102.
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=TV1338 {ECO:0000305};
GN   ORFNames=TVG1381191 {ECO:0000312|EMBL:BAB60480.1};
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Methanobacteriati; Thermoplasmatota; Thermoplasmata;
OC   Thermoplasmatales; Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND MUTAGENESIS OF GLU-418 AND GLU-571.
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
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=48.7 mM for trehalose {ECO:0000269|PubMed:25979886};
CC         Note=kcat is 63.0 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 3.3 to 4.0). {ECO:0000269|PubMed:25979886};
CC       Temperature dependence:
CC         Optimum temperature is 60 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; BA000011; BAB60480.1; -; Genomic_DNA.
DR   RefSeq; WP_241760278.1; NC_002689.2.
DR   AlphaFoldDB; Q978S7; -.
DR   SMR; Q978S7; -.
DR   STRING; 273116.gene:9382146; -.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   PaxDb; 273116-gene:9382146; -.
DR   GeneID; 1441455; -.
DR   KEGG; tvo:TVG1381191; -.
DR   eggNOG; arCOG03286; Archaea.
DR   HOGENOM; CLU_010399_2_0_2; -.
DR   OMA; AACQFQL; -.
DR   PhylomeDB; Q978S7; -.
DR   BRENDA; 3.2.1.28; 6326.
DR   UniPathway; UPA00300; UER00535.
DR   Proteomes; UP000001017; Chromosome.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; EXP:UniProtKB.
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   PANTHER; PTHR31616:SF0; GLUCAN 1,4-ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR31616; TREHALASE; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   Pfam; PF19291; TREH_N; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..623
FT                   /note="Trehalase"
FT                   /id="PRO_0000448959"
FT   MUTAGEN         418
FT                   /note="E->Q: Less than 1% of wild-type activity."
FT                   /evidence="ECO:0000269|PubMed:25979886"
FT   MUTAGEN         571
FT                   /note="E->Q: 4% of wild-type activity."
FT                   /evidence="ECO:0000269|PubMed:25979886"
SQ   SEQUENCE   623 AA;  71827 MW;  D2734498519B7DF0 CRC64;
     MKKIPHELTH MAFHGLVKYS DITVEGYPKI QYHGFIGNNR TAMLVAMNGY IDWGCLPNFN
     SNAVFSSILD KNKGGYFAIF PSDTTDVYVD QYYKEMTNVL VTEFVKNGKI ILRLTDFMPD
     SEYGKISFPE VHRFVESFSE PIDITIDFKP TFNYGQDKPI IEKDQHGFIF TTDKESIGIS
     SEFPLRKNSD RIFGNVKMEP RSSSWIIALY GIHHLFRTTD YKSYLRLQET TDYWRKWASS
     SSYAGAYHSM VMRSALALKV LFYEPTGLMV AAPTASLPEA IGGERNWDYR FTWIRDTAYV
     IEALSSIGYK YEATEFLYDM MDMITRDNRI RTIYSIDDSN DLEERIIDYE GYRGSRPVRI
     GNKAVDQLQI DQYGSIVRAI HSMAKAGGIV NSYLWDFVEQ VMAKIEYLWK YPDSSIWEFR
     TEPKQYVYSK VMSWAAFDSA ISMAKDLGLS APIKQWKSIQ DEIKKEVLEK GFDTDTNSFV
     QYYGSKNIDA ALLRLPILGF IPANDEKFLG TLSRIEKELM VDGYLFKRYR EDDGLKGDEG
     SFLMLTFWYI EDLILMKRLK KAREVLESVL EKANHLGLYS EEIDEKSGDF LGNFPQALSH
     LGVIRVAPKL EEALLKRTSK INS
//