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Reviewed, UniProtKB/Swiss-Prot O32462 (MALQ_THELI)

Last modified November 25, 2008. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    4-alpha-glucanotransferase
    EC=2.4.1.25
Alternative name(s):
    Amylomaltase
    Disproportionating enzyme
      Short name=D-enzyme
Gene names
Name: jgt
OrganismThermococcus litoralis
Taxonomic identifier2265 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

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Protein attributes

Sequence length659 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the transglycosylation of maltooligosaccharides, yielding maltooligosaccharides of various lengths and glucose.

Catalytic activity

Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.

Enzyme regulation

Inhibited by p-chloromercuribenzoic acid, monoiodoacetic acid, mercury and nickel ions.

Sequence similarities

Belongs to the glycosyl hydrolase 57 family.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 90 degrees Celsius.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6596594-alpha-glucanotransferase
PRO_0000184577

Sites

Active site1231Nucleophile
Active site2141Proton donor

Secondary structure

1 .............................................................................................................. 659
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O32462-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F789AFF9BF8281AC

FASTA65977,885
        10         20         30         40         50         60 
MERINFIFGI HNHQPLGNFG WVFEEAYNRS YRPFMEILEE FPEMKVNVHF SGPLLEWIEE 

        70         80         90        100        110        120 
NKPDYLDLLR SLIKRGQLEI VVAGFYEPVL AAIPKEDRLV QIEMLKDYAR KLGYDAKGVW 

       130        140        150        160        170        180 
LTERVWQPEL VKSLREAGIE YVVVDDYHFM SAGLSKEELF WPYYTEDGGE VITVFPIDEK 

       190        200        210        220        230        240 
LRYLIPFRPV KKTIEYLESL TSDDPSKVAV FHDDGEKFGV WPGTYEWVYE KGWLREFFDA 

       250        260        270        280        290        300 
ITSNEKINLM TYSEYLSKFT PRGLVYLPIA SYFEMSEWSL PAKQAKLFVE FVEQLKEEGK 

       310        320        330        340        350        360 
FEKYRVFVRG GIWKNFFFKY PESNFMHKRM LMVSKAVRDN PEARKYILKA QCNDAYWHGV 

       370        380        390        400        410        420 
FGGIYLPHLR RTVWENIIKA QRYLKPENKI LDVDFDGRAE IMVENDGFIA TIKPHYGGSI 

       430        440        450        460        470        480 
FELSSKRKAV NYNDVLPRRW EHYHEVPEAT KPEKESEEGI ASIHELGKQI PEEIRRELAY 

       490        500        510        520        530        540 
DWQLRAILQD HFIKPEETLD NYRLVKYHEL GDFVNQPYEY EMIENGVKLW REGGVYAEEK 

       550        560        570        580        590        600 
IPARVEKKIE LTEDGFIAKY RVLLEKPYKA LFGVEINLAV HSVMEKPEEF EAKEFEVNDP 

       610        620        630        640        650 
YGIGKVRIEL DKAAKVWKFP IKTLSQSEAG WDFIQQGVSY TMLFPIEKEL EFTVRFREL

« Hide

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References

[1]"4-alpha-glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis. Enzyme purification and characterization, and gene cloning, sequencing and expression in Escherichia coli."
Jeon B.-S., Taguchi H., Sakai H., Ohshima T., Wakagi T., Matsuzawa H.
Eur. J. Biochem. 248:171-178(1997) [PubMed: 9310375] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19 AND 427-437, CHARACTERIZATION.
Strain: DSM 5473.
[2]"Crystal structures of 4-alpha-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor."
Imamura H., Fushinobu S., Yamamoto M., Kumasaka T., Jeon B.S., Wakagi T., Matsuzawa H.
J. Biol. Chem. 278:19378-19386(2003) [PubMed: 12618437] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

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Cross-references

Sequence databases

D88253 Genomic DNA. Translation: BAA22063.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1K1WX-ray2.80A1-659[»]
1K1XX-ray2.40A/B1-659[»]
1K1YX-ray2.40A/B1-659[»]
ModBaseSearch...

Family and domain databases

InterProIPR015179. a-amylase/a-glucanoTrfase_prok.
IPR015178. DUF1925.
IPR004300. Glyco_hydro_57_core.
[Graphical view]
PfamPF09094. DUF1925. 1 hit.
PF09095. DUF1926. 1 hit.
PF03065. Glyco_hydro_57. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameMALQ_THELI
AccessionPrimary (citable) accession number: O32462
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 1, 1998
Last modified: November 25, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents