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O32462 (MALQ_THELN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. 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:
4-alpha-glucanotransferase

EC=2.4.1.25
Alternative name(s):
Amylomaltase
Disproportionating enzyme
Short name=D-enzyme
Gene names
Name:jgt
ORF Names:OCC_10078
OrganismThermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) [Complete proteome] [HAMAP]
Taxonomic identifier523849 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length659 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transglycosylation of maltooligosaccharides, yielding maltooligosaccharides of various lengths and glucose. Maltose and glucose can be used as acceptors in the transfer reaction. Ref.3

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. Ref.3

Enzyme regulation

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

Subunit structure

homodimer. Ref.3

Induction

Expressed constitutively. Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 57 family.

Biophysicochemical properties

Kinetic parameters:

Vmax=13 µmol/min/mg enzyme with maltose as substrate Ref.3

Vmax=26 µmol/min/mg enzyme with maltotriose as substrate

Temperature dependence:

Optimum temperature is 85-100 degrees Celsius.

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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
O32462 [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

References

« Hide 'large scale' 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19 AND 427-437, CHARACTERIZATION.
Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
[2]"Genome sequence of the model hyperthermophilic archaeon Thermococcus litoralis NS-C."
Gardner A.F., Kumar S., Perler F.B.
J. Bacteriol. 194:2375-2376(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
[3]"Maltose metabolism in the hyperthermophilic archaeon Thermococcus litoralis: purification and characterization of key enzymes."
Xavier K.B., Peist R., Kossmann M., Boos W., Santos H.
J. Bacteriol. 181:3358-3367(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-35, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION.
Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
[4]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88253 Genomic DNA. Translation: BAA22063.1.
CP006670 Genomic DNA. Translation: EHR79231.1.
RefSeqYP_008428452.1. NC_022084.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K1WX-ray2.80A1-659[»]
1K1XX-ray2.40A/B1-659[»]
1K1YX-ray2.40A/B1-659[»]
ProteinModelPortalO32462.
SMRO32462. Positions 2-659.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH57. Glycoside Hydrolase Family 57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID16548782.
KEGGtlt:OCC_10078.

Organism-specific databases

CMRSearch...

Enzyme and pathway databases

BRENDA2.4.1.25. 6302.

Family and domain databases

Gene3D2.70.98.10. 1 hit.
3.20.110.10. 2 hits.
InterProIPR015179. A-amylase/a-glucTrfase_C.
IPR015178. A-amylase/a-glucTrfase_central.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR028995. Glyco_hydro_57/38_cen.
IPR004300. Glyco_hydro_57_N.
[Graphical view]
PfamPF09094. DUF1925. 1 hit.
PF09095. DUF1926. 1 hit.
PF03065. Glyco_hydro_57. 1 hit.
[Graphical view]
ProDomPD014405. DUF1925. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO32462.

Entry information

Entry nameMALQ_THELN
AccessionPrimary (citable) accession number: O32462
Secondary accession number(s): H3ZLH6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries