ID   TREH2_SULAC             Reviewed;         576 AA.
AC   Q4J9D4;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Trehalase 2 {ECO:0000303|PubMed:29574614};
DE            EC=3.2.1.28 {ECO:0000269|PubMed:29574614};
DE   AltName: Full=Alpha,alpha-trehalase {ECO:0000305};
DE   AltName: Full=SaTreH2 {ECO:0000303|PubMed:29574614};
GN   Name=treH2; OrderedLocusNames=Saci_1250 {ECO:0000312|EMBL:AAY80596.1};
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-8, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=29574614; DOI=10.1007/s00253-018-8915-7;
RA   Yuasa M., Okamura T., Kimura M., Honda S., Shin Y., Kawakita M., Oyama F.,
RA   Sakaguchi M.;
RT   "Two trehalose-hydrolyzing enzymes from Crenarchaeon Sulfolobus
RT   acidocaldarius exhibit distinct activities and affinities toward
RT   trehalose.";
RL   Appl. Microbiol. Biotechnol. 102:4445-4455(2018).
CC   -!- FUNCTION: Catalyzes the hydrolysis of alpha,alpha-trehalose into two
CC       molecules of D-glucose. {ECO:0000269|PubMed:29574614}.
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:29574614};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.39 mM for trehalose (at 50 degrees Celsius and pH 3.7)
CC         {ECO:0000269|PubMed:29574614};
CC         KM=3.47 mM for trehalose (at 70 degrees Celsius and pH 3.7)
CC         {ECO:0000269|PubMed:29574614};
CC         Note=kcat is 1.60 sec(-1) at 50 degrees Celsius and pH 3.7. kcat is
CC         3.43 sec(-1) at 70 degrees Celsius and pH 3.7.
CC         {ECO:0000269|PubMed:29574614};
CC       pH dependence:
CC         Optimum pH is 3.7. More than half of the maximal activity is observed
CC         over a range between pH 3.5 and 4.5. {ECO:0000269|PubMed:29574614};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.
CC         {ECO:0000269|PubMed:29574614};
CC   -!- PATHWAY: Glycan degradation; trehalose degradation; D-glucose from
CC       alpha,alpha-trehalose: step 1/1. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR   EMBL; CP000077; AAY80596.1; -; Genomic_DNA.
DR   RefSeq; WP_011278098.1; NC_007181.1.
DR   AlphaFoldDB; Q4J9D4; -.
DR   SMR; Q4J9D4; -.
DR   STRING; 330779.Saci_1250; -.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   EnsemblBacteria; AAY80596; AAY80596; Saci_1250.
DR   GeneID; 3473722; -.
DR   KEGG; sai:Saci_1250; -.
DR   PATRIC; fig|330779.12.peg.1212; -.
DR   eggNOG; arCOG03286; Archaea.
DR   HOGENOM; CLU_010399_3_1_2; -.
DR   OMA; VEWMCVP; -.
DR   UniPathway; UPA00300; UER00535.
DR   Proteomes; UP000001018; 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; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..576
FT                   /note="Trehalase 2"
FT                   /id="PRO_0000448958"
SQ   SEQUENCE   576 AA;  66574 MW;  F0C79B58970059D4 CRC64;
     MNYALLSNGI TTALEKEGSI EWFPVPKFDS PSVFTKILDE DKGGYFLITP EKFNKVKQQY
     VEYSLILRTE FDDGNLILID FLPLSLPAII RLYEAKVPFN VEVKPLFNYG LVNAGTETRK
     DGIIYKNPES KEGLELLING DYKIISPYRI TVNSGKGYLY LLYSRDLRYG LFSQKGFVYS
     EPYEAYSKLL YYSRKELERA RKPSIYENAF YRSLSVILGL IYKPSGGIIA SPTTSIPEIV
     GDERNWDYRY VWVRDSSYAI EALVKANLLT HARRALDFLT NLLDPSSKSF DHPFYSVDGT
     PPPAEENLDW LSGFMNSKPV RIGNAAYLQI QMDIEGAYMN ALYEYYKRTL DKDYISSIFW
     AVEAISDWVS SSWRGESTDI WEERGISRHY THTKLMSWVA LDRASKLAKD LGYNKLFEEW
     KSRANEIKID ILNNGVKDNH HFVRYYGGDE IDAALLTLPI YDFIPATDTL FMNTLKKIDE
     ELRVADGLYL RYKKDFMGLA KNPFTLVTTW MARVYIRLKE FDRARWLLET LIKCNQDLGL
     IGEHVDPETC EARGNYPHLF PHSGMVLSIL EFDEVR