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Q55088 (TREZ_SULSF) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Malto-oligosyltrehalose trehalohydrolase
Short name=MTHase
EC=3.2.1.141
Alternative name(s):
4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase
Glycosyltrehalose trehalohydrolase
Short name=GTHase
Maltooligosyl trehalose trehalohydrolase
Gene names
Name:treZ
OrganismSulfolobus solfataricus
Taxonomic identifier2287 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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.

Pathway

Glycan biosynthesis; trehalose biosynthesis.

Subunit structure

Homodimer. Ref.3

Subcellular location

Cytoplasm Ref.2.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processtrehalose biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559Malto-oligosyltrehalose trehalohydrolase
PRO_0000393751

Regions

Region309 – 3135Substrate binding By similarity

Sites

Active site2531Nucleophile By similarity
Active site2841Proton donor By similarity
Site3781Transition state stabilizer By similarity

Experimental info

Mutagenesis2991C → V: Reduces activity by 50%. No change in substrate specificity. Ref.3

Secondary structure

1 .................................................................. 559
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q55088 [UniParc].

Last modified May 1, 1997. Version 2.
Checksum: 79FBE23A7CD38B4E

FASTA55964,790
        10         20         30         40         50         60 
MTFAYKIDGN EVIFTLWAPY QKSVKLKVLE KGLYEMERDE KGYFTITLNN VKVRDRYKYV 

        70         80         90        100        110        120 
LDDASEIPDP ASRYQPEGVH GPSQIIQESK EFNNETFLKK EDLIIYEIHV GTFTPEGTFE 

       130        140        150        160        170        180 
GVIRKLDYLK DLGITAIEIM PIAQFPGKRD WGYDGVYLYA VQNSYGGPEG FRKLVDEAHK 

       190        200        210        220        230        240 
KGLGVILDVV YNHVGPEGNY MVKLGPYFSQ KYKTPWGLTF NFDDAESDEV RKFILENVEY 

       250        260        270        280        290        300 
WIKEYNVDGF RLDAVHAIID TSPKHILEEI ADVVHKYNRI VIAESDLNDP RVVNPKEKCG 

       310        320        330        340        350        360 
YNIDAQWVDD FHHSIHAYLT GERQGYYTDF GNLDDIVKSY KDVFVYDGKY SNFRRKTHGE 

       370        380        390        400        410        420 
PVGELDGCNF VVYIQNHDQV GNRGKGERII KLVDRESYKI AAALYLLSPY IPMIFMGEEY 

       430        440        450        460        470        480 
GEENPFYFFS DFSDSKLIQG VREGRKKENG QDTDPQDEST FNASKLSWKI DEEIFSFYKI 

       490        500        510        520        530        540 
LIKMRKELSI ACDRRVNVVN GENWLIIKGR EYFSLYVFSK SSIEVKYSGT LLLSSNNSFP 

       550 
QHIEEGKYEF DKGFALYKL

« Hide

References

[1]"Gene cloning and expression of new trehalose-producing enzymes from the hyperthermophilic archaeum Sulfolobus solfataricus KM1."
Kobayashi K., Kato M., Miura Y., Kettoku M., Komeda T., Iwamatsu A.
Biosci. Biotechnol. Biochem. 60:1882-1885(1996) [PubMed: 8987868] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: KM1.
[2]"Purification and characterization of new trehalose-producing enzymes isolated from the hyperthermophilic archae, Sulfolobus solfataricus KM1."
Kato M., Miura Y., Kettoku M., Shindo K., Iwamatsu A., Kobayashi K.
Biosci. Biotechnol. Biochem. 60:546-550(1996) [PubMed: 8901122] [Abstract]
Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.
Strain: KM1.
[3]"Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus."
Feese M.D., Kato Y., Tamada T., Kato M., Komeda T., Miura Y., Hirose M., Hondo K., Kobayashi K., Kuroki R.
J. Mol. Biol. 301:451-464(2000) [PubMed: 10926520] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-558, SUBUNIT, MUTAGENESIS OF CYS-299.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D64130 Genomic DNA. Translation: BAA11010.1.
PIRJC5135.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EH9X-ray3.00A2-558[»]
1EHAX-ray3.00A2-558[»]
ProteinModelPortalQ55088.
SMRQ55088. Positions 2-558.
ModBaseSearch...

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR015902. Alpha_amylase.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR015156. Maltooligo_trehalose_arc_C.
IPR012768. Trehalose_TreZ.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PTHR10357:SF21. PTHR10357:SF21. 1 hit.
PfamPF09071. Alpha-amyl_C. 1 hit.
PF00128. Alpha-amylase. 2 hits.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFPIRSF006337. Trehalose_TreZ. 1 hit.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.
TIGRFAMsTIGR02402. Trehalose_TreZ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTREZ_SULSF
AccessionPrimary (citable) accession number: Q55088
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: May 1, 1997
Last modified: November 16, 2011
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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