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Q93HU3 (GLGB_RHOMR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 72. 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:
1,4-alpha-glucan branching enzyme GlgB

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
Glycogen branching enzyme
Short name=BE
Gene names
Name:glgB
OrganismRhodothermus marinus (Rhodothermus obamensis)
Taxonomic identifier29549 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeRhodothermus

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position By similarity. HAMAP-Rule MF_00685

Catalytic activity

Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain. HAMAP-Rule MF_00685

Pathway

Glycan biosynthesis; glycogen biosynthesis. HAMAP-Rule MF_00685

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00685

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6216211,4-alpha-glucan branching enzyme GlgB HAMAP-Rule MF_00685
PRO_0000188737

Sites

Active site3051Nucleophile By similarity
Active site3561Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q93HU3 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1F93D30FFB29697A

FASTA62172,238
        10         20         30         40         50         60 
MSWLTEEDIR RWESGTFYDS YRKLGAHPDD EGTWFCVWAP HADGVSVLGA FNDWNPEANP 

        70         80         90        100        110        120 
LERYGGGLWA GYVPGARPGH TYKYRIRHGF YQADKTDPYA FAMEPPTGSP IEGLASIITR 

       130        140        150        160        170        180 
LDYTWHDDEW MRRRKGPASL YEPVSIYEVH LGSWRHKRPG ESFSYREIAE PLADYVQEMG 

       190        200        210        220        230        240 
FTHVELLPVM EHPYYGSWGY QVVGYYAPTF RYGSPQDLMY LIDYLHQRGI GVILDWVPSH 

       250        260        270        280        290        300 
FAADPQGLVF FDGTTLFEYD DPKMRYHPDW GTYVFDYNKP GVRNFLISNA LFWLEKYHVD 

       310        320        330        340        350        360 
GLRVDAVASM LYRDYSRKEW TPNIFGGREN LEAIDFIKKF NETVYLHFPE AMTIAEESTA 

       370        380        390        400        410        420 
WPGVSAPTYN NGLGFLYKWN MGWMHDTLDY IQRDPIYRKY HHDELTFSLW YAFSEHYVLP 

       430        440        450        460        470        480 
LSHDEVVHGK GSLWGKMPGD DWQKAANLRL LFGHMWGHPG KKLLFMGGEF GQHHEWNHDT 

       490        500        510        520        530        540 
QLEWHLLDQP YHRGIQLWVC DLNHLYRTNP ALWHDGPEGF EWIDFSDRDQ SVICYLRKNA 

       550        560        570        580        590        600 
GRMLLFVLNF TPVPREHYRV GVPIGGPWHE VLNSDAVAYG GSGMGNFGRV EAVPESWHGR 

       610        620 
PFHLELTLPP LAALILEPEH G 

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References

[1]"A novel thermostable branching enzyme from an extremely thermophilic bacterial species, Rhodothermus obamensis."
Shinohara M.L., Ihara M., Abo M., Hashida M., Takagi S., Beck T.C.
Appl. Microbiol. Biotechnol. 57:653-659(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB060080 Genomic DNA. Translation: BAB69858.1.

3D structure databases

ProteinModelPortalQ93HU3.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00164.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
HAMAPMF_00685. GlgB.
InterProIPR006048. A-amylase_b_C.
IPR006407. GlgB.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 2 hits.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFPIRSF000463. GlgB. 1 hit.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsTIGR01515. branching_enzym. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLGB_RHOMR
AccessionPrimary (citable) accession number: Q93HU3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 72 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries