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Q44315 (TREY_ARTSQ) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Maltooligosyl trehalose synthase

EC=5.4.99.15
Alternative name(s):
(1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase
Gene names
Name:treY
OrganismArthrobacter sp. (strain Q36)
Taxonomic identifier104027 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length775 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of maltooligosaccharide into the non-reducing saccharide, maltooligosyl trehalose (alpha-maltooligosyl alpha-D-glucoside) by intramolecular transglycosylation.

Catalytic activity

4-((1->4)-alpha-D-glucosyl)(n-1)-D-glucose = 1-alpha-D-((1->4)-alpha-D-glucosyl)(n-1)-alpha-D-glucopyranoside.

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 775775Maltooligosyl trehalose synthase
PRO_0000054341

Sequences

Sequence LengthMass (Da)Tools
Q44315 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 1BBD23024B2280FC

FASTA77585,356
        10         20         30         40         50         60 
MRTPVSTYRL QIRKGFTLFD AAKTVPYLHS LGVDWVYLSP VLTAEQGSDH GYDVTDPSAV 

        70         80         90        100        110        120 
DPERGGPEGL AAVSKAARAA GMGVLIDIVP NHVGVATPAQ NPWWWSLLKE GRQSRYAEAF 

       130        140        150        160        170        180 
DVDWDLAGGR IRLPVLGSDD DLDQLEIRDG ELRYYDHRFP LAEGTYAEGD APRDVHARQH 

       190        200        210        220        230        240 
YELIGWRRAD NELNYRRFFA VNTLAGVRVE IPAVFDEAHQ EVVRWFREDL ADGLRIDHPD 

       250        260        270        280        290        300 
GLADPEGYLK RLREVTGGAY LLIEKILEPG EQLPASFECE GTTGYDALAD VDRVLVDPRG 

       310        320        330        340        350        360 
QEPLDRLDAS LRGGEPADYQ DMIRGTKRRI TDGILHSEIL RLARLVPGDA NVSIDAGADA 

       370        380        390        400        410        420 
LAEIIAAFPV YRTYLPEGAE VLKEACELAA RRRPELDQAI QALQPLLLDT DLELARRFQQ 

       430        440        450        460        470        480 
TSGMVMAKGV EDTAFFRYNR LGTLTEVGAD PTEFAVEPDE FHARLARRQA ELPLSMTTLS 

       490        500        510        520        530        540 
THDTKRSEDT RARISVISEV AGDWEKALNR LRDLAPLPDG PLSALLWQAI AGAWPASRER 

       550        560        570        580        590        600 
LQYYALKAAR EAGNSTNWTD PAPAFEEKLK AAVDAVFDNP AVQAEVEALV ELLEPYGASN 

       610        620        630        640        650        660 
SLAAKLVQLT MPGVPDVYQG TEFWDRSLTD PDNRRPFSFD DRRAALEQLD AGDLPASFTD 

       670        680        690        700        710        720 
ERTKLLVTSR ALRLRRDRPE LFTGYRPVLA SGPAAGHLLA FDRGTAAAPG ALTLATRLPY 

       730        740        750        760        770 
GLEQSGGWRD TAVELNTAMK DELTGAGFGP GAVKIADIFR SFPVALLVPQ TGGES 

« 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: 8605217] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobacter sp. Q36."
Nakada T., Maruta K., Tsusaki K., Kubota M., Chaen H., Sugimoto T., Kurimoto M., Tsujisaka Y.
Biosci. Biotechnol. Biochem. 59:2210-2214(1995) [PubMed: 8611744] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63343 Genomic DNA. Translation: BAA09667.1.
PIRS65769.

3D structure databases

ProteinModelPortalQ44315.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-6021.

Family and domain databases

InterProIPR015902. Alpha_amylase.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013797. Maltooligo_trehalose_synth_N.
IPR012767. Trehalose_TreY.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 4 hits.
G3DSA:1.10.10.470. Maltooligo_trehalose_synth_N. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
TIGRFAMsTIGR02401. Trehalose_TreY. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTREY_ARTSQ
AccessionPrimary (citable) accession number: Q44315
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 1, 1996
Last modified: September 21, 2011
This is version 62 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

SIMILARITY comments

Index of protein domains and families