TREZ_SACSO
ID TREZ_SACSO Reviewed; 559 AA.
AC Q55088;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Malto-oligosyltrehalose trehalohydrolase;
DE Short=MTHase;
DE EC=3.2.1.141 {ECO:0000269|PubMed:22334583};
DE AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase;
DE AltName: Full=Glycosyltrehalose trehalohydrolase;
DE Short=GTHase;
DE AltName: Full=Maltooligosyl trehalose trehalohydrolase;
GN Name=treZ;
OS Saccharolobus solfataricus (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KM1;
RX PubMed=8987868; DOI=10.1271/bbb.60.1882;
RA Kobayashi K., Kato M., Miura Y., Kettoku M., Komeda T., Iwamatsu A.;
RT "Gene cloning and expression of new trehalose-producing enzymes from the
RT hyperthermophilic archaeum Sulfolobus solfataricus KM1.";
RL Biosci. Biotechnol. Biochem. 60:1882-1885(1996).
RN [2]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RC STRAIN=KM1;
RX PubMed=8901122; DOI=10.1271/bbb.60.546;
RA Kato M., Miura Y., Kettoku M., Shindo K., Iwamatsu A., Kobayashi K.;
RT "Purification and characterization of new trehalose-producing enzymes
RT isolated from the hyperthermophilic archae, Sulfolobus solfataricus KM1.";
RL Biosci. Biotechnol. Biochem. 60:546-550(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-558, SUBUNIT, AND MUTAGENESIS OF
RP CYS-299.
RX PubMed=10926520; DOI=10.1006/jmbi.2000.3977;
RA Feese M.D., Kato Y., Tamada T., Kato M., Komeda T., Miura Y., Hirose M.,
RA Hondo K., Kobayashi K., Kuroki R.;
RT "Crystal structure of glycosyltrehalose trehalohydrolase from the
RT hyperthermophilic archaeum Sulfolobus solfataricus.";
RL J. Mol. Biol. 301:451-464(2000).
RN [4] {ECO:0007744|PDB:3VGB, ECO:0007744|PDB:3VGD, ECO:0007744|PDB:3VGE, ECO:0007744|PDB:3VGF, ECO:0007744|PDB:3VGG, ECO:0007744|PDB:3VGH}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, CATALYTIC
RP ACTIVITY, SUBUNIT, MUTAGENESIS OF ASP-253 AND GLU-284, AND ACTIVE SITE.
RX PubMed=22334583; DOI=10.1002/pro.2039;
RA Okazaki N., Tamada T., Feese M.D., Kato M., Miura Y., Komeda T.,
RA Kobayashi K., Kondo K., Blaber M., Kuroki R.;
RT "Substrate recognition mechanism of a glycosyltrehalose trehalohydrolase
RT from Sulfolobus solfataricus KM1.";
RL Protein Sci. 21:539-552(2012).
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:22334583};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000305|PubMed:22334583, ECO:0000305|PubMed:8901122}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10926520,
CC ECO:0000269|PubMed:22334583}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8901122}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; D64130; BAA11010.1; -; Genomic_DNA.
DR PIR; JC5135; JC5135.
DR PDB; 1EH9; X-ray; 3.00 A; A=2-559.
DR PDB; 1EHA; X-ray; 3.00 A; A=2-559.
DR PDB; 3VGB; X-ray; 2.65 A; A=2-559.
DR PDB; 3VGD; X-ray; 2.40 A; A=2-559.
DR PDB; 3VGE; X-ray; 2.70 A; A=2-559.
DR PDB; 3VGF; X-ray; 2.30 A; A=2-559.
DR PDB; 3VGG; X-ray; 2.66 A; A=2-559.
DR PDB; 3VGH; X-ray; 2.60 A; A=2-559.
DR PDBsum; 1EH9; -.
DR PDBsum; 1EHA; -.
DR PDBsum; 3VGB; -.
DR PDBsum; 3VGD; -.
DR PDBsum; 3VGE; -.
DR PDBsum; 3VGF; -.
DR PDBsum; 3VGG; -.
DR PDBsum; 3VGH; -.
DR AlphaFoldDB; Q55088; -.
DR SMR; Q55088; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR BRENDA; 3.2.1.141; 6163.
DR UniPathway; UPA00299; -.
DR EvolutionaryTrace; Q55088; -.
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; 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 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 3D-structure; Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase.
FT CHAIN 1..559
FT /note="Malto-oligosyltrehalose trehalohydrolase"
FT /id="PRO_0000393751"
FT ACT_SITE 253
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:22334583"
FT ACT_SITE 284
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:22334583"
FT BINDING 251..256
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22334583"
FT BINDING 309..313
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22334583"
FT BINDING 377..382
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22334583"
FT SITE 378
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:22334583"
FT MUTAGEN 253
FT /note="D->E: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22334583"
FT MUTAGEN 284
FT /note="E->Q: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22334583"
FT MUTAGEN 299
FT /note="C->V: Reduces activity by 50%. No change in
FT substrate specificity."
FT /evidence="ECO:0000269|PubMed:10926520"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:3VGF"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1EHA"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3VGE"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 227..245
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 325..329
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:3VGF"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 377..381
FT /evidence="ECO:0007829|PDB:3VGF"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:1EH9"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 395..406
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 435..449
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 458..463
FT /evidence="ECO:0007829|PDB:3VGF"
FT HELIX 472..487
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 502..508
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 529..537
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:3VGF"
FT STRAND 552..557
FT /evidence="ECO:0007829|PDB:3VGF"
SQ SEQUENCE 559 AA; 64790 MW; 79FBE23A7CD38B4E CRC64;
MTFAYKIDGN EVIFTLWAPY QKSVKLKVLE KGLYEMERDE KGYFTITLNN VKVRDRYKYV
LDDASEIPDP ASRYQPEGVH GPSQIIQESK EFNNETFLKK EDLIIYEIHV GTFTPEGTFE
GVIRKLDYLK DLGITAIEIM PIAQFPGKRD WGYDGVYLYA VQNSYGGPEG FRKLVDEAHK
KGLGVILDVV YNHVGPEGNY MVKLGPYFSQ KYKTPWGLTF NFDDAESDEV RKFILENVEY
WIKEYNVDGF RLDAVHAIID TSPKHILEEI ADVVHKYNRI VIAESDLNDP RVVNPKEKCG
YNIDAQWVDD FHHSIHAYLT GERQGYYTDF GNLDDIVKSY KDVFVYDGKY SNFRRKTHGE
PVGELDGCNF VVYIQNHDQV GNRGKGERII KLVDRESYKI AAALYLLSPY IPMIFMGEEY
GEENPFYFFS DFSDSKLIQG VREGRKKENG QDTDPQDEST FNASKLSWKI DEEIFSFYKI
LIKMRKELSI ACDRRVNVVN GENWLIIKGR EYFSLYVFSK SSIEVKYSGT LLLSSNNSFP
QHIEEGKYEF DKGFALYKL
