TREH_THEVO
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 25-MAY-2022, entry version 90.
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 ORFNames=TVG1381191 {ECO:0000312|EMBL:BAB60480.1};
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC 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 AlphaFoldDB; Q978S7; -.
DR SMR; Q978S7; -.
DR STRING; 273116.14325577; -.
DR CAZy; GH15; Glycoside Hydrolase Family 15.
DR EnsemblBacteria; BAB60480; BAB60480; BAB60480.
DR KEGG; tvo:TVG1381191; -.
DR eggNOG; arCOG03286; Archaea.
DR HOGENOM; CLU_010399_2_0_2; -.
DR OMA; VEWMCVP; -.
DR PhylomeDB; Q978S7; -.
DR UniPathway; UPA00300; UER00535.
DR Proteomes; UP000001017; 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; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosidase; Hydrolase.
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