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Q5JDJ7 (BE_THEKO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
1,4-alpha-glucan branching enzyme TK1436

EC=2.4.1.18
Alternative name(s):
1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase
Alpha-(1->4)-glucan branching enzyme
Branching enzyme
Short name=BE
Gene names
Ordered Locus Names:TK1436
OrganismThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) [Reference proteome] [HAMAP]
Taxonomic identifier69014 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length675 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 5 to 30, with two local maxima at DP 6 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Does not display alpha-galactosidase or pullulanase activity, since melibiose and pullulan are not substrates. Is not able to catalyze the hydrolysis or transglycosylation of maltoheptaose, suggesting that the TK1436 protein contains neither alpha-amylase nor 4-alpha-glucanotransferase activity. Ref.2

Catalytic activity

Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain. Ref.2

Subunit structure

Monomer. Ref.2 Ref.3

Induction

Up-regulated by maltodextrin. Ref.2

Domain

The C-terminus contains two copies of a helix-hairpin-helix (HhH) motif that are dispensable for activity and thermal stability. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 57 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0. Ref.2

Temperature dependence:

Optimum temperature is 70 degrees Celsius. Is thermostable up to 90 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6756751,4-alpha-glucan branching enzyme TK1436
PRO_0000413973

Sites

Active site1831Nucleophile Ref.3
Active site3541Proton donor Ref.3
Binding site2611Substrate
Binding site2781Substrate; via amide nitrogen
Binding site4071Substrate
Binding site4671Substrate
Binding site4761Substrate
Site2331Transition state stabilizer Probable

Secondary structure

............................................................................................ 675
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5JDJ7 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 857E34E04F23B27A

FASTA67578,549
        10         20         30         40         50         60 
MKGYLTFVLH THIPYVRKHG KWPFGEEWVF EAISETYIPL LMEFERLRDS GVKFGIVINV 

        70         80         90        100        110        120 
TPVLAEQLTD EYMKKAFEEY MERKLKAMEE DLKSGKYDEK AVSYMLNYFR KVYDYWKAIN 

       130        140        150        160        170        180 
GDIIGKLREL QDQGYVEVIT SAATHGYLPL LGRDEAIRAQ IANGVATYEK HFGMKPKGIW 

       190        200        210        220        230        240 
LPECAYRPAG EWELPGGRKV KRQGIEKFLE EFGLRYFFVE SRLIDEGPAS NVYGEVLIAD 

       250        260        270        280        290        300 
TEKTTLRPYW IKGSNVAVFA RNRETGHQVW SAHYGYPGDF WYREFHKKAP KSGGQYWRIT 

       310        320        330        340        350        360 
SKEVGLGEKE FYDPDKAMER VEEHARHFVS LVERLLREHE EKFGEKGIIV APYDTELFGH 

       370        380        390        400        410        420 
WWFEGVKWLG RVLELLYQRG VETPTLSRFL EEYSGEKHEI ELPEGSWGAN SDHSTWWNEE 

       430        440        450        460        470        480 
TEWTWPHIYR AEDRMVAIVS RFRGRDELTN RVIEQLAREL LILEASDWQF LITTGQAKEY 

       490        500        510        520        530        540 
AKRRVLIHSR DFHRLANELV RYVKIGEFDV KLLEELEERD NPFRPVVVGP YVSENPPELE 

       550        560        570        580        590        600 
EYVEPPEVPP EKEETEEKPK VLTEKATSLA LAVKKVKPVK EETREVKKKA VEASKRGKRK 

       610        620        630        640        650        660 
SSKSKRLPRK VSKKAPSKGP SDLLSIKGIG PKTFQKLKRA GVETIEDLKN ANIEDLARKT 

       670 
GISTKRLKKF IAQVE 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-918 / JCM 12380 / KOD1.
[2]"A novel branching enzyme of the GH-57 family in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1."
Murakami T., Kanai T., Takata H., Kuriki T., Imanaka T.
J. Bacteriol. 188:5915-5924(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBUNIT, DOMAIN.
Strain: ATCC BAA-918 / JCM 12380 / KOD1.
[3]"Structural basis for branching-enzyme activity of glycoside hydrolase family 57: structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1."
Santos C.R., Tonoli C.C., Trindade D.M., Betzel C., Takata H., Kuriki T., Kanai T., Imanaka T., Arni R.K., Murakami M.T.
Proteins 79:547-557(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 1-562 OF APOENZYME AND IN COMPLEXES WITH GLUCOSE AND SUBSTRATE ANALOGS, SUBUNIT, ACTIVE SITES.
Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006878 Genomic DNA. Translation: BAD85625.1.
RefSeqYP_183849.1. NC_006624.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3N8TX-ray2.40A1-562[»]
3N92X-ray2.89A1-562[»]
3N98X-ray1.87A1-562[»]
ProteinModelPortalQ5JDJ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING69014.TK1436.

Protein family/group databases

CAZyGH57. Glycoside Hydrolase Family 57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD85625; BAD85625; TK1436.
GeneID3234278.
KEGGtko:TK1436.

Phylogenomic databases

eggNOGCOG1543.
HOGENOMHOG000046905.
OMAAFFGRDS.

Enzyme and pathway databases

BioCycTKOD69014:GH72-1461-MONOMER.
BRENDA2.4.1.18. 264868.

Family and domain databases

Gene3D1.20.1430.10. 1 hit.
3.20.110.10. 1 hit.
InterProIPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
IPR015293. DUF1957.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR028995. Glyco_hydro_57/38_cen.
IPR004300. Glyco_hydro_57_N.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
[Graphical view]
PfamPF09210. DUF1957. 1 hit.
PF03065. Glyco_hydro_57. 1 hit.
[Graphical view]
SMARTSM00278. HhH1. 2 hits.
[Graphical view]
SUPFAMSSF47794. SSF47794. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ5JDJ7.

Entry information

Entry nameBE_THEKO
AccessionPrimary (citable) accession number: Q5JDJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: February 15, 2005
Last modified: June 11, 2014
This is version 65 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