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Q8FQ12 (GLGB_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. 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:CE1323
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length731 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 – 7317311,4-alpha-glucan branching enzyme GlgB HAMAP-Rule MF_00685
PRO_0000188698

Sites

Active site4081Nucleophile By similarity
Active site4611Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FQ12 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 63B5690B96EDBB4E

FASTA73182,714
        10         20         30         40         50         60 
MTPASANDLL IPEEDLNRLR HCHHHNPHGF YGWHATDDGS VIRTRQIGAE KVELVLGDTQ 

        70         80         90        100        110        120 
IVMNPIGDDI FAIKLGNREA FDYRLRVTWP GQDPVVTADP YIFLPTLGEM DTYLISEGRH 

       130        140        150        160        170        180 
ERLWDVLGAN VKTYETTLGQ VRGTAFAVWA PNAIGVAVIG GFNGWNASQH AMRSLGGSGI 

       190        200        210        220        230        240 
WELFIPNIGP GEVYKFAIQT REGHRRDKAD PMARLAELPP ATGSIVVESD YQWQDSEWMD 

       250        260        270        280        290        300 
KRAEIDTATT PMSVYEVHLG SWRWGRSYAE LATELVDYVA DLGYTHVEFM PVAEHPFGGS 

       310        320        330        340        350        360 
WGYQVSGYYA PTSRWGSPDE LRKLIDAFHA RGIGVIIDWV PAHFPKDDWA LARFDGQALY 

       370        380        390        400        410        420 
EHPDWRRGEQ KDWGTYVFNF GRSEVRNFLV ANALYWLEEF HVDGLRVDAV ASMLYLDYSR 

       430        440        450        460        470        480 
EHGEWEPNVY GGRENLEAVQ FLQEMNATVQ RVHPGALTIA EESTSWPGVT APTWDGGLGF 

       490        500        510        520        530        540 
SLKWNMGWMN DTLEYFSKDP IHRSFHHNEL TFSLVYAFSE RFVLPISHDE VVHGKGSLWN 

       550        560        570        580        590        600 
RMPGDTWNKA AGMRTLLAYM WAHPGKKLLF MGQEIGQRDE WSEAHELPWG VVEGWQGEYH 

       610        620        630        640        650        660 
EGISDLVREL NSTYKEVTAL HQRDFSGEGF TWNKADDASN NILVFTRHGD DGSQALCVFN 

       670        680        690        700        710        720 
LSGTSQPEYQ IGVSGGGSWR LVLNTDDEQY HGANNPLPET IEAEKIDRDG FPYTTTLHSP 

       730 
AMSAQFYVWE G 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC18133.1.
RefSeqNP_737933.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FQ12.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE1323.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC18133; BAC18133; BAC18133.
GeneID1033641.
KEGGcef:CE1323.
PATRIC21488782. VBICorEff9312_1324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000283037.
KOK00700.
OMAISEGRHE.
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. 1 hit.
[Graphical view]
PIRSFPIRSF000463. GlgB. 1 hit.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 2 hits.
TIGRFAMsTIGR01515. branching_enzym. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLGB_COREF
AccessionPrimary (citable) accession number: Q8FQ12
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: March 1, 2003
Last modified: June 11, 2014
This is version 81 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