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P95867 (TREZ_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Maltooligosyl trehalose trehalohydrolase
Gene names
Name:treZ
Ordered Locus Names:SSO2093
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length561 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 By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Biophysicochemical properties

Kinetic parameters:

KM=7.22 mM for maltotriosyltrehalose Ref.3

KM=5.66 mM for maltotetraosyltrehalose

KM=5.89 mM for maltopentaosyltrehalose

KM=5.86 mM for maltopentaose

KM=5.63 mM for maltohexaose

KM=2.63 mM for maltoheptaose

pH dependence:

Optimum pH is 5.0.

Temperature dependence:

Optimum temperature is 85 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
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 – 561561Malto-oligosyltrehalose trehalohydrolase
PRO_0000393752

Regions

Region311 – 3155Substrate binding By similarity

Sites

Active site2551Nucleophile
Active site2861Proton donor
Site3801Transition state stabilizer

Experimental info

Mutagenesis2181W → F or A: 15-fold and 150-fold reduction in specific activity, respectively. Ref.3
Mutagenesis2551D → A: 660-fold reduction in specific activity. Ref.3
Mutagenesis2591A → S: Insignificant change in specific activity. Ref.3
Mutagenesis2861E → A: 1100-fold reduction in specific activity. Ref.3
Mutagenesis3281Y → F: 2-fold reduction in specific activity. Ref.3
Mutagenesis3551F → Y: Very small decrease in specific activity. Ref.3
Mutagenesis3561R → K: 2-fold reduction in specific activity. Ref.3
Mutagenesis3801D → A: 8140-fold reduction in specific activity. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P95867 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: B00E403020F6B242

FASTA56164,371
        10         20         30         40         50         60 
MTFGYKLDED GVTFNLWAPY QRKVKLKILN RGIYEMERDD KGYFTITLDN VRVGDRYKYI 

        70         80         90        100        110        120 
LDDNSEVPDP ASRYQPEGVH GYSEIISPDF EWDDENSVKV KREDLVIYEL HIGTFTSEGT 

       130        140        150        160        170        180 
FEGVIKKLNY LKELGVTAIE IMPIAQFPGK KDWGYDGVYL YAVQNSYGGP SGFRKLVNEA 

       190        200        210        220        230        240 
HKLGLAVILD VVYNHVGPEG NYMVKLGPYF SEKYKTPWGL TFNFDDAGSD EVRKFILENV 

       250        260        270        280        290        300 
EYWINEFHVD GFRLDAVHAI IDNSPKHILE DIADVVHKYD KIVIAESDLN DPRVVNPKEK 

       310        320        330        340        350        360 
CGYNIDAQWV DDFHHAIHAF LTGERQGYYS DFGSIGDIVK SYKDVFIYDG KYSNFRRKTH 

       370        380        390        400        410        420 
GKSVGDLDGC KFVVYIQNHD QVGNRGGGER LIKLVDKESY KIAAALYILS PYIPMIFMGE 

       430        440        450        460        470        480 
EYGEENPFYY FSDFSDPKLI QGVREGRRRE NGQETDPQSD CTFNDSKLSW KINDDILSFY 

       490        500        510        520        530        540 
KSLIKIRKEY GLACNRKLSV ENGNYWLTVK GNGCLAVYVF SKSVIEMKYS GTLVLSSNSS 

       550        560 
FPSQITESKY ELDKGFALYK L

« Hide

References

« Hide 'large scale' references
[1]"Organizational characteristics and information content of an archaeal genome: 156 kb of sequence from Sulfolobus solfataricus P2."
Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y., Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F., Ragan M.A., Charlebois R.L.
Mol. Microbiol. 22:175-191(1996) [PubMed: 8899719] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[2]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed: 11427726] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[3]"Identification of the essential catalytic residues and selectivity-related residues of maltooligosyltrehalose trehalohydrolase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092."
Fang T.Y., Tseng W.C., Shih T.Y., Wang M.Y.
J. Agric. Food Chem. 56:5628-5633(2008) [PubMed: 18563901] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF TRP-218; ASP-255; ALA-259; GLU-286; TYR-328; PHE-355; ARG-356 AND ASP-380.
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y08256 Genomic DNA. Translation: CAA69503.1.
AE006641 Genomic DNA. Translation: AAK42272.1.
PIRS73087.
RefSeqNP_343482.1. NC_002754.1.

3D structure databases

HSSPHSSP built from PDB template 1EH9 based on UniProtKB Q55088.
ProteinModelPortalP95867.
SMRP95867. Positions 2-560.
ModBaseSearch...

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1453599.
GenomeReviewsGene locus SSO2093 in contig AE006641_GR.
KEGGsso:SSO2093.
NMPDRfig|273057.1.peg.1905.

Phylogenomic databases

HOGENOMHBG367595.
OMAEGFVYQG.
ProtClustDBCLSK285578.

Enzyme and pathway databases

BioCycSSOL273057:SSO2093-MONOMER.
BRENDA3.2.1.141. 6163.

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_SULSO
AccessionPrimary (citable) accession number: P95867
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: May 1, 1997
Last modified: November 16, 2011
This is version 79 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents