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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)DescriptionActionsGraphical viewLength
Active sitei253Nucleophile1 Publication1
Active sitei284Proton donor1 Publication1
Sitei378Transition state stabilizer1 Publication1

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)DescriptionActionsGraphical viewLength
Mutagenesisi253D → E: Abolishes enzyme activity. 1 Publication1
Mutagenesisi284E → Q: Abolishes enzyme activity. 1 Publication1
Mutagenesisi299C → V: Reduces activity by 50%. No change in substrate specificity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003937511 – 559Malto-oligosyltrehalose trehalohydrolaseAdd BLAST559

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1559
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Beta strandi11 – 17Combined sources7
Beta strandi25 – 28Combined sources4
Turni29 – 31Combined sources3
Beta strandi32 – 35Combined sources4
Beta strandi43 – 50Combined sources8
Beta strandi56 – 60Combined sources5
Beta strandi76 – 78Combined sources3
Beta strandi79 – 81Combined sources3
Helixi100 – 102Combined sources3
Beta strandi105 – 108Combined sources4
Helixi110 – 113Combined sources4
Beta strandi114 – 116Combined sources3
Helixi119 – 124Combined sources6
Helixi126 – 132Combined sources7
Beta strandi136 – 139Combined sources4
Beta strandi146 – 148Combined sources3
Beta strandi157 – 161Combined sources5
Helixi163 – 165Combined sources3
Helixi167 – 180Combined sources14
Beta strandi184 – 189Combined sources6
Beta strandi196 – 198Combined sources3
Helixi201 – 203Combined sources3
Beta strandi208 – 214Combined sources7
Beta strandi217 – 220Combined sources4
Beta strandi222 – 224Combined sources3
Helixi227 – 245Combined sources19
Beta strandi249 – 253Combined sources5
Helixi255 – 257Combined sources3
Beta strandi262 – 264Combined sources3
Helixi266 – 276Combined sources11
Beta strandi280 – 284Combined sources5
Helixi290 – 292Combined sources3
Helixi296 – 298Combined sources3
Beta strandi304 – 307Combined sources4
Helixi309 – 320Combined sources12
Helixi325 – 329Combined sources5
Helixi333 – 342Combined sources10
Beta strandi347 – 351Combined sources5
Turni352 – 355Combined sources4
Beta strandi356 – 358Combined sources3
Helixi367 – 369Combined sources3
Beta strandi370 – 372Combined sources3
Helixi377 – 381Combined sources5
Turni382 – 385Combined sources4
Helixi389 – 391Combined sources3
Helixi395 – 406Combined sources12
Beta strandi408 – 415Combined sources8
Helixi418 – 420Combined sources3
Helixi435 – 449Combined sources15
Helixi458 – 463Combined sources6
Helixi472 – 487Combined sources16
Beta strandi497 – 500Combined sources4
Beta strandi502 – 508Combined sources7
Beta strandi513 – 519Combined sources7
Beta strandi521 – 525Combined sources5
Beta strandi529 – 537Combined sources9
Beta strandi541 – 543Combined sources3
Beta strandi545 – 550Combined sources6
Beta strandi552 – 557Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ55088.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni251 – 256Substrate binding1 Publication6
Regioni309 – 313Substrate binding1 Publication5
Regioni377 – 382Substrate binding1 Publication6

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
PDB 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.
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: November 2, 2016
This is version 92 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.