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Q8DLB8 (GLGB_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 82. 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
Ordered Locus Names:tll0578
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length766 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 – 7667661,4-alpha-glucan branching enzyme GlgB HAMAP-Rule MF_00685
PRO_0000188754

Sites

Active site4311Nucleophile By similarity
Active site4841Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DLB8 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 42ED3BCF9036035E

FASTA76689,885
        10         20         30         40         50         60 
MTVSPEQIDR IVSNQHHDPF EILGCHQIQQ NGQSVWAVRA YLPNAERVSV LCPEQRQEYP 

        70         80         90        100        110        120 
MTPVHHPHFF ECHIPVAELN NYQLKIYENG HERVIYDPYA FRSPKLTDFD IHLFAEGNHH 

       130        140        150        160        170        180 
RIYEKLGAHL LTVDGVEGVY FAVWAPNARN VSVIGDFNHW DGRKHQMARR GNGIWELFIP 

       190        200        210        220        230        240 
GLSVGERYKY EIKNQEGHIY EKSDPYGFYQ EPRPKTASIV TDLNSYEWGD SDWLEKRRHT 

       250        260        270        280        290        300 
DPLNQPISVY EVHLGSWLHA SMEDPPIGAD GQPQEPVQAA ELKPWARFLT YRELAAKLIP 

       310        320        330        340        350        360 
YVKELGYTHI ELLPVAEHPF DGSWGYQVTG YYAPTSRYGS PHDFMYFVDQ CHQNGIGVIV 

       370        380        390        400        410        420 
DWVPGHFPKD GHGLAFFDGT HLYEHADPRK GEHKEWGTLV FNYGRHEVRN FLVANALFWF 

       430        440        450        460        470        480 
DKYHIDGIRV DAVASMLYLD YGRKEGEWIP NEYGGRENLE AANFLRQVNH VIFSYFPGIL 

       490        500        510        520        530        540 
SIAEESTAWP MVSWPTYMGG LGFNLKWNMG WMHDMLDYFS MDPWFRQFHH NNVTFSMWYH 

       550        560        570        580        590        600 
HSENFMLALS HDEVVHGKSH IIGKMPGDRW QKFANLRCLF AYMFTHPGKK TMFMGMEFAQ 

       610        620        630        640        650        660 
WSEWNVWSDL EWHLLQYEPH QQIKRFFGDL NHLYRSQPAL YSQDFKQEGF EWIDCSDNRH 

       670        680        690        700        710        720 
SVVSFIRWDK DYQDFVVVVC NFTPQPHSHY RIGVPEHGFY RELFNSDARE YGGSNMGNLG 

       730        740        750        760 
GKWADEWPYH QRRYSLDLCL PPLAVLILKL DREKTVAERA RYNLQS 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC08130.1.
RefSeqNP_681368.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DLB8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tll0578.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC08130; BAC08130; BAC08130.
GeneID1012543.
KEGGtel:tll0578.
PATRIC23926416. VBITheElo119873_0610.

Phylogenomic databases

eggNOGCOG0296.
HOGENOMHOG000283037.
KOK00700.
OMAAKLLFMG.
OrthoDBEOG6JX7GT.

Enzyme and pathway databases

UniPathwayUPA00164.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
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. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 2 hits.
[Graphical view]
PIRSFPIRSF000463. GlgB. 1 hit.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 2 hits.
TIGRFAMsTIGR01515. branching_enzym. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLGB_THEEB
AccessionPrimary (citable) accession number: Q8DLB8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: March 1, 2003
Last modified: June 11, 2014
This is version 82 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