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Protein

Malto-oligosyltrehalose trehalohydrolase

Gene

treZ

Organism
Sulfolobus solfataricus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to yield trehalose and (1->4)-alpha-D-glucan.1 Publication

Pathwayi: trehalose biosynthesis

This protein is involved in the pathway trehalose biosynthesis, which is part of Glycan biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in the pathway trehalose biosynthesis and in Glycan biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei253 – 2531Nucleophile1 Publication
Active sitei284 – 2841Proton donor1 Publication
Sitei378 – 3781Transition state stabilizer1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BRENDAi3.2.1.141. 6163.
UniPathwayiUPA00299.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Malto-oligosyltrehalose trehalohydrolase (EC:3.2.1.1411 Publication)
Short name:
MTHase
Alternative name(s):
4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase
Glycosyltrehalose trehalohydrolase
Short name:
GTHase
Maltooligosyl trehalose trehalohydrolase
Gene namesi
Name:treZ
OrganismiSulfolobus solfataricus
Taxonomic identifieri2287 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi253 – 2531D → E: Abolishes enzyme activity. 1 Publication
Mutagenesisi284 – 2841E → Q: Abolishes enzyme activity. 1 Publication
Mutagenesisi299 – 2991C → V: Reduces activity by 50%. No change in substrate specificity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Malto-oligosyltrehalose trehalohydrolasePRO_0000393751Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
559
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Beta strandi11 – 177Combined sources
Beta strandi25 – 284Combined sources
Turni29 – 313Combined sources
Beta strandi32 – 354Combined sources
Beta strandi43 – 508Combined sources
Beta strandi56 – 605Combined sources
Beta strandi76 – 783Combined sources
Beta strandi79 – 813Combined sources
Helixi100 – 1023Combined sources
Beta strandi105 – 1084Combined sources
Helixi110 – 1134Combined sources
Beta strandi114 – 1163Combined sources
Helixi119 – 1246Combined sources
Helixi126 – 1327Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi157 – 1615Combined sources
Helixi163 – 1653Combined sources
Helixi167 – 18014Combined sources
Beta strandi184 – 1896Combined sources
Beta strandi196 – 1983Combined sources
Helixi201 – 2033Combined sources
Beta strandi208 – 2147Combined sources
Beta strandi217 – 2204Combined sources
Beta strandi222 – 2243Combined sources
Helixi227 – 24519Combined sources
Beta strandi249 – 2535Combined sources
Helixi255 – 2573Combined sources
Beta strandi262 – 2643Combined sources
Helixi266 – 27611Combined sources
Beta strandi280 – 2845Combined sources
Helixi290 – 2923Combined sources
Helixi296 – 2983Combined sources
Beta strandi304 – 3074Combined sources
Helixi309 – 32012Combined sources
Helixi325 – 3295Combined sources
Helixi333 – 34210Combined sources
Beta strandi347 – 3515Combined sources
Turni352 – 3554Combined sources
Beta strandi356 – 3583Combined sources
Helixi367 – 3693Combined sources
Beta strandi370 – 3723Combined sources
Helixi377 – 3815Combined sources
Turni382 – 3854Combined sources
Helixi389 – 3913Combined sources
Helixi395 – 40612Combined sources
Beta strandi408 – 4158Combined sources
Helixi418 – 4203Combined sources
Helixi435 – 44915Combined sources
Helixi458 – 4636Combined sources
Helixi472 – 48716Combined sources
Beta strandi497 – 5004Combined sources
Beta strandi502 – 5087Combined sources
Beta strandi513 – 5197Combined sources
Beta strandi521 – 5255Combined sources
Beta strandi529 – 5379Combined sources
Beta strandi541 – 5433Combined sources
Beta strandi545 – 5506Combined sources
Beta strandi552 – 5576Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EH9X-ray3.00A2-559[»]
1EHAX-ray3.00A2-559[»]
3VGBX-ray2.65A2-559[»]
3VGDX-ray2.40A2-559[»]
3VGEX-ray2.70A2-559[»]
3VGFX-ray2.30A2-559[»]
3VGGX-ray2.66A2-559[»]
3VGHX-ray2.60A2-559[»]
ProteinModelPortaliQ55088.
SMRiQ55088. Positions 2-558.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ55088.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni251 – 2566Substrate binding1 Publication
Regioni309 – 3135Substrate binding1 Publication
Regioni377 – 3826Substrate binding1 Publication

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR015156. Maltooligo_trehalose_arc_C.
IPR012768. Trehalose_TreZ.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF09071. Alpha-amyl_C. 1 hit.
PF00128. Alpha-amylase. 2 hits.
[Graphical view]
PIRSFiPIRSF006337. Trehalose_TreZ. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR02402. trehalose_TreZ. 1 hit.

Sequencei

Sequence statusi: Complete.

Q55088-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTFAYKIDGN EVIFTLWAPY QKSVKLKVLE KGLYEMERDE KGYFTITLNN
60 70 80 90 100
VKVRDRYKYV LDDASEIPDP ASRYQPEGVH GPSQIIQESK EFNNETFLKK
110 120 130 140 150
EDLIIYEIHV GTFTPEGTFE GVIRKLDYLK DLGITAIEIM PIAQFPGKRD
160 170 180 190 200
WGYDGVYLYA VQNSYGGPEG FRKLVDEAHK KGLGVILDVV YNHVGPEGNY
210 220 230 240 250
MVKLGPYFSQ KYKTPWGLTF NFDDAESDEV RKFILENVEY WIKEYNVDGF
260 270 280 290 300
RLDAVHAIID TSPKHILEEI ADVVHKYNRI VIAESDLNDP RVVNPKEKCG
310 320 330 340 350
YNIDAQWVDD FHHSIHAYLT GERQGYYTDF GNLDDIVKSY KDVFVYDGKY
360 370 380 390 400
SNFRRKTHGE PVGELDGCNF VVYIQNHDQV GNRGKGERII KLVDRESYKI
410 420 430 440 450
AAALYLLSPY IPMIFMGEEY GEENPFYFFS DFSDSKLIQG VREGRKKENG
460 470 480 490 500
QDTDPQDEST FNASKLSWKI DEEIFSFYKI LIKMRKELSI ACDRRVNVVN
510 520 530 540 550
GENWLIIKGR EYFSLYVFSK SSIEVKYSGT LLLSSNNSFP QHIEEGKYEF

DKGFALYKL
Length:559
Mass (Da):64,790
Last modified:May 1, 1997 - v2
Checksum:i79FBE23A7CD38B4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64130 Genomic DNA. Translation: BAA11010.1.
PIRiJC5135.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64130 Genomic DNA. Translation: BAA11010.1.
PIRiJC5135.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EH9X-ray3.00A2-559[»]
1EHAX-ray3.00A2-559[»]
3VGBX-ray2.65A2-559[»]
3VGDX-ray2.40A2-559[»]
3VGEX-ray2.70A2-559[»]
3VGFX-ray2.30A2-559[»]
3VGGX-ray2.66A2-559[»]
3VGHX-ray2.60A2-559[»]
ProteinModelPortaliQ55088.
SMRiQ55088. Positions 2-558.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00299.
BRENDAi3.2.1.141. 6163.

Miscellaneous databases

EvolutionaryTraceiQ55088.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR015156. Maltooligo_trehalose_arc_C.
IPR012768. Trehalose_TreZ.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF09071. Alpha-amyl_C. 1 hit.
PF00128. Alpha-amylase. 2 hits.
[Graphical view]
PIRSFiPIRSF006337. Trehalose_TreZ. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR02402. trehalose_TreZ. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTREZ_SULSF
AccessioniPrimary (citable) accession number: Q55088
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: May 1, 1997
Last modified: July 6, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.