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B9J2G8 (GLGB_BACCQ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 44. 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:BCQ_4685
OrganismBacillus cereus (strain Q1) [Complete proteome] [HAMAP]
Taxonomic identifier361100 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length645 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 – 6456451,4-alpha-glucan branching enzyme GlgB HAMAP-Rule MF_00685
PRO_1000147758

Sites

Active site3091Nucleophile By similarity
Active site3521Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
B9J2G8 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: BB622B9A824E9ABA

FASTA64575,926
        10         20         30         40         50         60 
MSVINCEEVK RDEFHTEKYY ESYNIFGAHI VTEDEMRGVR FTVWAPHAKA MSVVGDFNEW 

        70         80         90        100        110        120 
DYEQHKMLQV TEEGIWSLFI PHIEEREIYK YAIETMAGDV ILKADPYAVY AEVRPNTASV 

       130        140        150        160        170        180 
VFDIKGYEWN DKNWSRKKKK KSVYKEAMTV YELHFGSWKK KEDGTLYSYR EMAEELIPYV 

       190        200        210        220        230        240 
VEHQFTHIEI MPLVEHPYDR SWGYQGTGYY AATSRFGTPH DLMHFVDECH KYGIGVILDW 

       250        260        270        280        290        300 
VPGHFCKDAH GLYLFDGTPT YEYKDKDVQE NPVWGTVNFD LGKREVRNFL ISNALFWMRY 

       310        320        330        340        350        360 
FHIDGFRVDA VANMLYWNKE GQEQSNEHAV SFLRELNEAV FAEDEDFLMT AEDSTAWPLV 

       370        380        390        400        410        420 
TAPTYEGGLG FNYKWNMGWM NDVLKYMECA PEYRKYIHDK MTFSLLYAYS ENFILPLSHD 

       430        440        450        460        470        480 
EVVHGKKSLL NKMPGDYWDK FAQLRLLYGY FFTHPGKKLL FMGGEFGQFD EWKDLEDLDW 

       490        500        510        520        530        540 
NLHDFEMHRY MHDYFKELIA LYKRSKPLWQ LDHSPEGFQW IDANNNEQSI FSFIRQGDKQ 

       550        560        570        580        590        600 
EDALVVVCNF TKATYENYKV GVPDFEYYNE ILNSDAEQYG GSGQVNKKRL KAIQEPYHNQ 

       610        620        630        640 
AAHVEITIPP FGVSILRPVK TRKGSKKQDG SKTKVRSNVT SRGKR 

« Hide

References

[1]"Complete genome sequence of the extremophilic Bacillus cereus strain Q1 with industrial applications."
Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X., Xue Y., Zhu Y., Jin Q.
J. Bacteriol. 191:1120-1121(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Q1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000227 Genomic DNA. Translation: ACM15111.1.
RefSeqYP_002532400.1. NC_011969.1.

3D structure databases

ProteinModelPortalB9J2G8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING361100.BCQ_4685.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM15111; ACM15111; BCQ_4685.
GeneID7373696.
KEGGbcq:BCQ_4685.
PATRIC18917165. VBIBacCer120424_4747.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0296.
HOGENOMHOG000283037.
KOK00700.
OMAAKLLFMG.
OrthoDBEOG6JX7GT.

Enzyme and pathway databases

BioCycBCER361100:GJ7M-4673-MONOMER.
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.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFPIRSF000463. GlgB. 1 hit.
SUPFAMSSF51445. SSF51445. 1 hit.
TIGRFAMsTIGR01515. branching_enzym. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLGB_BACCQ
AccessionPrimary (citable) accession number: B9J2G8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: June 11, 2014
This is version 44 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