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Q5SH28 (BE_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 TTHA1902

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:TTHA1902
ORF Names:TT1467
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length520 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 3 to 13, with two local maxima at DP 7 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Is involved in glycogen biosynthesis. Shows a secondary activity, i.e. the hydrolysis of the substrate, being 4% of the total activity. Can use amylose as substrate but not alpha-1,4-linked oligosaccharides of 2-7 glucose residues, beta-cyclodextrin, 6-O-glucosyl-beta-cyclodextrin and 6-O-maltosyl-beta-cyclodextrin. Is not able to branch amylopectin further, it only hydrolyzes amylopectin. Thus, displays preference for linear and long substrates (amylose) over branched structures (amylopectin). Ref.3

Catalytic activity

Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain. Ref.3

Pathway

Glycan biosynthesis; glycogen biosynthesis. Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 57 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.5. Ref.3

Temperature dependence:

Optimum temperature is 65 degrees Celsius. Remains fully active following incubation for 1 hour at 80 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5205201,4-alpha-glucan branching enzyme TTHA1902
PRO_0000413974

Sites

Active site1841Nucleophile
Active site3531Proton donor
Binding site2651Substrate By similarity
Binding site2821Substrate; via amide nitrogen By similarity
Binding site4041Substrate By similarity
Binding site4601Substrate By similarity
Binding site4691Substrate By similarity
Site2361Transition state stabilizer By similarity

Experimental info

Mutagenesis231F → A: Nearly no effect on enzymatic activity. Ref.3
Mutagenesis1841E → A: Complete loss of enzymatic activity. Binds amylose but not glycogen. Ref.3
Mutagenesis2361Y → A: Almost complete loss of branching activity but 10-fold increase in hydrolytic activity. Ref.3
Mutagenesis2711L → A: Nearly no effect on enzymatic activity. Ref.3
Mutagenesis2741W → A: 0.4% of wild-type enzymatic activity. Ref.3
Mutagenesis3531D → A: Complete loss of enzymatic activity. Ref.3
Mutagenesis3601W → A: 0.6% of wild-type enzymatic activity. Ref.3
Mutagenesis4041W → A: 0.4% of wild-type enzymatic activity. Ref.3
Mutagenesis4631F → A: 0.5% of wild-type enzymatic activity. Ref.3

Secondary structure

.......................................................................................... 520
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SH28 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 7B9C8668C760E259

FASTA52059,169
        10         20         30         40         50         60 
MARFALVLHA HLPYVRAHGM WPFGEETLYE AMAETYLPLI RVLERLRAEG VEAPFTLGIT 

        70         80         90        100        110        120 
PILAEQLADA RIKEGFWAYA KDRLERAQGD YQRYRGTALE ASARHQVAFW ELTLDHFQRL 

       130        140        150        160        170        180 
SGDLVAAFRK AEEGGQVELI TSNATHGYSP LLGYDEALWA QIKTGVSTYR RHFAKDPTGF 

       190        200        210        220        230        240 
WLPEMAYRPK GPWKPPVEGP PEGVRPGVDE LLMRAGIRYT FVDAHLVQGG EPLSPYGEAA 

       250        260        270        280        290        300 
LGPVESQEAT YHVHELESGL RVLARNPETT LQVWSADYGY PGEGLYREFH RKDPLSGLHH 

       310        320        330        340        350        360 
WRVTHRKADL AEKAPYDPEA AFAKTEEHAR HFVGLLERLA GRHPEGVILS PYDAELFGHW 

       370        380        390        400        410        420 
WYEGVAWLEA VLRLLAQNPK VRPVTAREAV QGPAVRTALP EGSWGRGGDH RVWLNEKTLD 

       430        440        450        460        470        480 
YWEKVYRAEG AMREAARRGV LPEGVLRQAM RELLLLEASD WPFLMETGQA EAYARERYEE 

       490        500        510        520 
HARAFFHLLK GASPEELRAL EERDNPFPEA DPRLYLFREA 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[2]"Crystal structure of TT1467 from Thermus thermophilus HB8."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"Thermus thermophilus glycoside hydrolase family 57 branching enzyme: crystal structure, mechanism of action, and products formed."
Palomo M., Pijning T., Booiman T., Dobruchowska J.M., van der Vlist J., Kralj S., Planas A., Loos K., Kamerling J.P., Dijkstra B.W., van der Maarel M.J., Dijkhuizen L., Leemhuis H.
J. Biol. Chem. 286:3520-3530(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, MUTAGENESIS OF PHE-23; GLU-184; TYR-236; LEU-271; TRP-274; ASP-353; TRP-360; TRP-404 AND PHE-463.
Strain: HB8 / ATCC 27634 / DSM 579.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008226 Genomic DNA. Translation: BAD71725.1.
RefSeqYP_145168.1. NC_006461.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UFAX-ray2.20A1-520[»]
3P0BX-ray1.35A1-520[»]
ProteinModelPortalQ5SH28.
SMRQ5SH28. Positions 1-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA1902.

Protein family/group databases

CAZyGH57. Glycoside Hydrolase Family 57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71725; BAD71725; BAD71725.
GeneID3167991.
KEGGttj:TTHA1902.
PATRIC23958769. VBITheThe93045_1870.

Phylogenomic databases

eggNOGCOG1543.
HOGENOMHOG000046905.
OMAAFFGRDS.
OrthoDBEOG6FNHJ7.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1948-MONOMER.
UniPathwayUPA00164.

Family and domain databases

Gene3D1.20.1430.10. 1 hit.
3.20.110.10. 1 hit.
InterProIPR015293. 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.
[Graphical view]
PfamPF09210. DUF1957. 1 hit.
PF03065. Glyco_hydro_57. 1 hit.
[Graphical view]
SUPFAMSSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ5SH28.

Entry information

Entry nameBE_THET8
AccessionPrimary (citable) accession number: Q5SH28
Secondary accession number(s): P84162
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: December 21, 2004
Last modified: June 11, 2014
This is version 52 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries