Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9AJN6 (TREZ_ARTRM) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 66. 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 ramosus
Taxonomic identifier1672 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length575 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: 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 – 575575Malto-oligosyltrehalose trehalohydrolase
PRO_0000054322

Regions

Region312 – 3165Substrate binding By similarity

Sites

Active site2501Nucleophile By similarity
Active site2871Proton donor By similarity
Site3821Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9AJN6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 284A3F20207E228B

FASTA57563,080
        10         20         30         40         50         60 
MNRRFPVWAP QAAQVTLVVG QGRAELPLTR DENGWWALQQ PWDGGPDLVD YGYLVDGKGP 

        70         80         90        100        110        120 
FADPRSLRQP RGVHELGREF DPARYAWGDD GWRGRDLTGA VIYELHVGTF TPEGTLDSAI 

       130        140        150        160        170        180 
RRLDHLVRLG VDAVELLPVN AFNGTHGWGY DGVLWYAVHE PYGGPEAYQR FVDACHARGL 

       190        200        210        220        230        240 
AVVQDVVYNH LGPSGNHLPD FGPYLGSGAA NTWGDALNLD GPLSDEVRRY IIDNAVYWLR 

       250        260        270        280        290        300 
DMHADGLRLD AVHALRDARA LHLLEELAAR VDELAGELGR PLTLIAESDL NDPKLIRSRA 

       310        320        330        340        350        360 
AHGYGLDAQW DDDVHHAVHA NVTGETVGYY ADFGGLGALV KVFQRGWFHD GTWSSFRERH 

       370        380        390        400        410        420 
HGRPLDPDIP FRRLVAFAQD HDQVGNRAVG DRMSAQVGEG SLAAAAALVL LGPFTPMLFM 

       430        440        450        460        470        480 
GEEWGARTPW QFFTSHPEPE LGEATARGRI AEFARMGWDP AVVPDPQDPA TFARSHLDWS 

       490        500        510        520        530        540 
EPEREPHAGL LAFYTDLIAL RRELPVDAPA REVDADEARG VFAFSRGPLR VTVALRPGPV 

       550        560        570 
GVPEHGGLVL AYGEVRAGAA GLHLDGPGAA IVRLE 

« Hide

References

[1]"Trehalose-producing operon treYZ from Arthrobacter ramosus S34."
Yamamoto T., Maruta K., Watanabe H., Yamashita H., Kubota M., Fukuda S., Kurimoto M.
Biosci. Biotechnol. Biochem. 65:1419-1423(2001) [PubMed: 11471747] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S34.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB045141 Genomic DNA. Translation: BAB40766.1.
PIRJC7727.

3D structure databases

ProteinModelPortalQ9AJN6.
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.
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.
IPR012768. Trehalose_TreZ.
[Graphical view]
Gene3DG3DSA: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.
PfamPF00128. 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_ARTRM
AccessionPrimary (citable) accession number: Q9AJN6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: June 1, 2001
Last modified: November 16, 2011
This is version 66 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