TREZ_SACS2
ID TREZ_SACS2 Reviewed; 561 AA.
AC P95867;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Malto-oligosyltrehalose trehalohydrolase;
DE Short=MTHase;
DE EC=3.2.1.141 {ECO:0000269|PubMed:18563901};
DE AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase;
DE AltName: Full=Maltooligosyl trehalose trehalohydrolase;
GN Name=treZ; OrderedLocusNames=SSO2093;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA Ragan M.A., Charlebois R.L.;
RT "Organizational characteristics and information content of an archaeal
RT genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL Mol. Microbiol. 22:175-191(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS
RP OF TRP-218; ASP-255; ALA-259; GLU-286; TYR-328; PHE-355; ARG-356 AND
RP ASP-380.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=18563901; DOI=10.1021/jf073320b;
RA Fang T.Y., Tseng W.C., Shih T.Y., Wang M.Y.;
RT "Identification of the essential catalytic residues and selectivity-related
RT residues of maltooligosyltrehalose trehalohydrolase from the thermophilic
RT archaeon Sulfolobus solfataricus ATCC 35092.";
RL J. Agric. Food Chem. 56:5628-5633(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-
CC [(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-
CC alpha-D-glucan.; EC=3.2.1.141;
CC Evidence={ECO:0000269|PubMed:18563901};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.22 mM for maltotriosyltrehalose {ECO:0000269|PubMed:18563901};
CC KM=5.66 mM for maltotetraosyltrehalose {ECO:0000269|PubMed:18563901};
CC KM=5.89 mM for maltopentaosyltrehalose {ECO:0000269|PubMed:18563901};
CC KM=5.86 mM for maltopentaose {ECO:0000269|PubMed:18563901};
CC KM=5.63 mM for maltohexaose {ECO:0000269|PubMed:18563901};
CC KM=2.63 mM for maltoheptaose {ECO:0000269|PubMed:18563901};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:18563901};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius.
CC {ECO:0000269|PubMed:18563901};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000305|PubMed:18563901}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18563901}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; Y08256; CAA69503.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK42272.1; -; Genomic_DNA.
DR PIR; S73087; S73087.
DR RefSeq; WP_009989788.1; NC_002754.1.
DR AlphaFoldDB; P95867; -.
DR SMR; P95867; -.
DR STRING; 273057.SSO2093; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAK42272; AAK42272; SSO2093.
DR GeneID; 44130795; -.
DR KEGG; sso:SSO2093; -.
DR PATRIC; fig|273057.12.peg.2171; -.
DR eggNOG; arCOG02951; Archaea.
DR HOGENOM; CLU_020726_2_0_2; -.
DR InParanoid; P95867; -.
DR OMA; FTPMLFM; -.
DR PhylomeDB; P95867; -.
DR BRENDA; 3.2.1.141; 6163.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033942; F:4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.10.760; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR015156; Maltooligo_trehalose_arc_C.
DR InterPro; IPR012768; Trehalose_TreZ.
DR InterPro; IPR044901; Trehalose_TreZ_E-set_sf.
DR Pfam; PF09071; Alpha-amyl_C; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
DR Pfam; PF02922; CBM_48; 1.
DR PIRSF; PIRSF006337; Trehalose_TreZ; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR02402; trehalose_TreZ; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW Reference proteome.
FT CHAIN 1..561
FT /note="Malto-oligosyltrehalose trehalohydrolase"
FT /id="PRO_0000393752"
FT ACT_SITE 255
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:18563901"
FT ACT_SITE 286
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:18563901"
FT BINDING 253..258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT BINDING 311..315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT BINDING 379..384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT SITE 380
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:18563901"
FT MUTAGEN 218
FT /note="W->F,A: 15-fold and 150-fold reduction in specific
FT activity, respectively."
FT /evidence="ECO:0000269|PubMed:18563901"
FT MUTAGEN 255
FT /note="D->A: 660-fold reduction in specific activity."
FT /evidence="ECO:0000269|PubMed:18563901"
FT MUTAGEN 259
FT /note="A->S: Insignificant change in specific activity."
FT /evidence="ECO:0000269|PubMed:18563901"
FT MUTAGEN 286
FT /note="E->A: 1100-fold reduction in specific activity."
FT /evidence="ECO:0000269|PubMed:18563901"
FT MUTAGEN 328
FT /note="Y->F: 2-fold reduction in specific activity."
FT /evidence="ECO:0000269|PubMed:18563901"
FT MUTAGEN 355
FT /note="F->Y: Very small decrease in specific activity."
FT /evidence="ECO:0000269|PubMed:18563901"
FT MUTAGEN 356
FT /note="R->K: 2-fold reduction in specific activity."
FT /evidence="ECO:0000269|PubMed:18563901"
FT MUTAGEN 380
FT /note="D->A: 8140-fold reduction in specific activity."
FT /evidence="ECO:0000269|PubMed:18563901"
SQ SEQUENCE 561 AA; 64371 MW; B00E403020F6B242 CRC64;
MTFGYKLDED GVTFNLWAPY QRKVKLKILN RGIYEMERDD KGYFTITLDN VRVGDRYKYI
LDDNSEVPDP ASRYQPEGVH GYSEIISPDF EWDDENSVKV KREDLVIYEL HIGTFTSEGT
FEGVIKKLNY LKELGVTAIE IMPIAQFPGK KDWGYDGVYL YAVQNSYGGP SGFRKLVNEA
HKLGLAVILD VVYNHVGPEG NYMVKLGPYF SEKYKTPWGL TFNFDDAGSD EVRKFILENV
EYWINEFHVD GFRLDAVHAI IDNSPKHILE DIADVVHKYD KIVIAESDLN DPRVVNPKEK
CGYNIDAQWV DDFHHAIHAF LTGERQGYYS DFGSIGDIVK SYKDVFIYDG KYSNFRRKTH
GKSVGDLDGC KFVVYIQNHD QVGNRGGGER LIKLVDKESY KIAAALYILS PYIPMIFMGE
EYGEENPFYY FSDFSDPKLI QGVREGRRRE NGQETDPQSD CTFNDSKLSW KINDDILSFY
KSLIKIRKEY GLACNRKLSV ENGNYWLTVK GNGCLAVYVF SKSVIEMKYS GTLVLSSNSS
FPSQITESKY ELDKGFALYK L
