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P30537 (GLGB_BACCL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. 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
OrganismBacillus caldolyticus
Taxonomic identifier1394 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length666 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is about 39 degrees Celsius. HAMAP-Rule MF_00685

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6666661,4-alpha-glucan branching enzyme GlgB HAMAP-Rule MF_00685
PRO_0000188677

Sites

Active site3091Nucleophile By similarity
Active site3521Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P30537 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 1F64C31495BB1B6E

FASTA66678,096
        10         20         30         40         50         60 
MIAANPTDLE VYLFHEGRLY QSYELFGAHV IRGGGAVGTR FCVWAPHARE VRLVGSFNDW 

        70         80         90        100        110        120 
NGTNSPLTKV NDEGVWTIVV PENLEGHLYK YEIITPDGRV LLKADPYAFY SELRPHTASI 

       130        140        150        160        170        180 
VYDLKGYEWN DSPWQRKKRR KRIYDQPMVI YELHFGSWKK KPDGRFYTYR EMADELIPYV 

       190        200        210        220        230        240 
LERGFTHIEL LPLVEHPLDR SWGYQGTGYY SVTSRYGTPH DFMYFVDRCH QAGLGVIIDW 

       250        260        270        280        290        300 
VPGHFCKDAH GLYMFDGAPT YEYANEKDRE NYVWGTANFD LGKPEVRSFL ISNALFWLEY 

       310        320        330        340        350        360 
YHVDGFRVDA VANMLYWPNN DRLYENPYAV EFLRQLNEAV FAYDPNVWMI AEDSTDWPRV 

       370        380        390        400        410        420 
TAPTYDGGLG FNYKWNMGWM NDMLKYMETP PHERKYAHNQ VSFSLLYAYS ENFILPFSHD 

       430        440        450        460        470        480 
EVVHGKKSLL NKMPGSYEEK FAQLRLLYGY MMAHPGKKLL FMGSEFAQFD EWKFAEELDW 

       490        500        510        520        530        540 
VLFDFELHRK MDEYVKQLIA CYKRYKPFYE LDHDPRGFEW IDVHNAEQSI FSFIRRGKKE 

       550        560        570        580        590        600 
GDVLVIVCNF TNQAYDDYKV SVPLLAPYRE VLNSDAAEFG GSGHVNGKRL PAFSEPFHGK 

       610        620        630        640        650        660 
PYHVRMTIPP FGISILRPVQ KRGERKQNEE EVHRHVIGRR ARKPASLADE KHRETSRAVW 


GEVPDH 

« Hide

References

[1]"The glgB gene from the thermophile Bacillus caldolyticus encodes a thermolabile branching enzyme."
Kiel J.A.K.W., Boels J.M., Beldman G., Venema G.
DNA Seq. 3:221-232(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z14057 Genomic DNA. Translation: CAA78440.1.
PIRB56639.

3D structure databases

ProteinModelPortalP30537.
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. 1 hit.
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_BACCL
AccessionPrimary (citable) accession number: P30537
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 11, 2014
This is version 85 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