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Q44316 (TREZ_ARTSQ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. 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

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
OrganismArthrobacter sp. (strain Q36)
Taxonomic identifier104027 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological_processtrehalose biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 598598Malto-oligosyltrehalose trehalohydrolase
PRO_0000054321

Regions

Region329 – 3335Substrate binding By similarity

Sites

Active site2671Nucleophile By similarity
Active site3041Proton donor By similarity
Site4001Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q44316 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8B5C610AD3766947

FASTA59865,832
        10         20         30         40         50         60 
MTHTYPREAA KPVLGPARYD VWAPNAESVT LLAGGERYAM QRRAETGPED AGWWTAAGAP 

        70         80         90        100        110        120 
TDGNVDYGYL LDGDETPLPD PRTRRQPDGV HALSRTFDPS AYSWQDDAWQ GRELQGAVIY 

       130        140        150        160        170        180 
ELHLGTFTPE GTLEAAAGKL DYLAGLGVDF IELLPVNAFN GTHNWGYDGV QWFAVHEAYG 

       190        200        210        220        230        240 
GPEAYQRFVD AAHAAGLGVI QDVVYNHLGP SGNYLPRFGP YLKQGEGNTW GDSVNLDGPG 

       250        260        270        280        290        300 
SDHVRRYILD NLAMWLRDYR VDGLRLDAVH ALKDERAVHI LEDFGALADQ ISAEVGRPLT 

       310        320        330        340        350        360 
LIAESDLNNP RLLYPRDVNG YGLEGQWSDD FHHAVHVNVT GETTGYYSDF DSLAALAKVL 

       370        380        390        400        410        420 
RDGFFHDGSY SSFRERHHGR PINFSAVHPA ALVVCSQNHD QIGNRATGDR LSQTLPYGSL 

       430        440        450        460        470        480 
ALAAVLTLTG PFTPMLLMGE EYGASTPWQF FTSHPEPELG KATAEGRIKE FERMGWDPAV 

       490        500        510        520        530        540 
VPDPQDPETF RRSKLDWAEA AEGDHARLLE LYRSLTALRR STPDLTKLGF EDTQVAFDED 

       550        560        570        580        590 
ARWLRFRRGG VQVLLNFSEQ PVSLDGAGTA LLLATDDAVR LEGERAELGP LSAAVVSD 

« Hide

References

[1]"Cloning and sequencing of trehalose biosynthesis genes from Arthrobacter sp. Q36."
Maruta K., Hattori K., Nakada T., Kubota M., Sugimoto T., Kurimoto M.
Biochim. Biophys. Acta 1289:10-13(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63343 Genomic DNA. Translation: BAA09668.1.
PIRS65770.

3D structure databases

ProteinModelPortalQ44316.
ModBaseSearch...

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-6022.
UniPathwayUPA00299.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.20.20.80. 2 hits.
InterProIPR022567. DUF3459.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR012768. Trehalose_TreZ.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PTHR10357:SF21. PTHR10357:SF21. 1 hit.
PfamPF00128. Alpha-amylase. 2 hits.
PF02922. CBM_48. 1 hit.
PF11941. DUF3459. 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_ARTSQ
AccessionPrimary (citable) accession number: Q44316
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 85 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