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B9J2G8

- GLGB_BACCQ

UniProt

B9J2G8 - GLGB_BACCQ

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Protein
1,4-alpha-glucan branching enzyme GlgB
Gene
glgB, BCQ_4685
Organism
Bacillus cereus (strain Q1)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei309 – 3091Nucleophile By similarity
Active sitei352 – 3521Proton donor By similarity

GO - Molecular functioni

  1. 1,4-alpha-glucan branching enzyme activity Source: UniProtKB-HAMAP
  2. cation binding Source: InterPro
  3. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

  1. glycogen biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism

Enzyme and pathway databases

BioCyciBCER361100:GJ7M-4673-MONOMER.
UniPathwayiUPA00164.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:glgB
Ordered Locus Names:BCQ_4685
OrganismiBacillus cereus (strain Q1)
Taxonomic identifieri361100 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000441: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6456451,4-alpha-glucan branching enzyme GlgBUniRule annotation
PRO_1000147758Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi361100.BCQ_4685.

Structurei

3D structure databases

ProteinModelPortaliB9J2G8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0296.
HOGENOMiHOG000283037.
KOiK00700.
OMAiAKLLFMG.
OrthoDBiEOG6JX7GT.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
HAMAPiMF_00685. GlgB.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFiPIRSF000463. GlgB. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR01515. branching_enzym. 1 hit.

Sequencei

Sequence statusi: Complete.

B9J2G8-1 [UniParc]FASTAAdd to Basket

« Hide

MSVINCEEVK RDEFHTEKYY ESYNIFGAHI VTEDEMRGVR FTVWAPHAKA    50
MSVVGDFNEW DYEQHKMLQV TEEGIWSLFI PHIEEREIYK YAIETMAGDV 100
ILKADPYAVY AEVRPNTASV VFDIKGYEWN DKNWSRKKKK KSVYKEAMTV 150
YELHFGSWKK KEDGTLYSYR EMAEELIPYV VEHQFTHIEI MPLVEHPYDR 200
SWGYQGTGYY AATSRFGTPH DLMHFVDECH KYGIGVILDW VPGHFCKDAH 250
GLYLFDGTPT YEYKDKDVQE NPVWGTVNFD LGKREVRNFL ISNALFWMRY 300
FHIDGFRVDA VANMLYWNKE GQEQSNEHAV SFLRELNEAV FAEDEDFLMT 350
AEDSTAWPLV TAPTYEGGLG FNYKWNMGWM NDVLKYMECA PEYRKYIHDK 400
MTFSLLYAYS ENFILPLSHD EVVHGKKSLL NKMPGDYWDK FAQLRLLYGY 450
FFTHPGKKLL FMGGEFGQFD EWKDLEDLDW NLHDFEMHRY MHDYFKELIA 500
LYKRSKPLWQ LDHSPEGFQW IDANNNEQSI FSFIRQGDKQ EDALVVVCNF 550
TKATYENYKV GVPDFEYYNE ILNSDAEQYG GSGQVNKKRL KAIQEPYHNQ 600
AAHVEITIPP FGVSILRPVK TRKGSKKQDG SKTKVRSNVT SRGKR 645
Length:645
Mass (Da):75,926
Last modified:March 24, 2009 - v1
Checksum:iBB622B9A824E9ABA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000227 Genomic DNA. Translation: ACM15111.1.
RefSeqiWP_000111390.1. NC_011969.1.
YP_002532400.1. NC_011969.1.

Genome annotation databases

EnsemblBacteriaiACM15111; ACM15111; BCQ_4685.
GeneIDi7373696.
KEGGibcq:BCQ_4685.
PATRICi18917165. VBIBacCer120424_4747.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000227 Genomic DNA. Translation: ACM15111.1 .
RefSeqi WP_000111390.1. NC_011969.1.
YP_002532400.1. NC_011969.1.

3D structure databases

ProteinModelPortali B9J2G8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 361100.BCQ_4685.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACM15111 ; ACM15111 ; BCQ_4685 .
GeneIDi 7373696.
KEGGi bcq:BCQ_4685.
PATRICi 18917165. VBIBacCer120424_4747.

Phylogenomic databases

eggNOGi COG0296.
HOGENOMi HOG000283037.
KOi K00700.
OMAi AKLLFMG.
OrthoDBi EOG6JX7GT.

Enzyme and pathway databases

UniPathwayi UPA00164 .
BioCyci BCER361100:GJ7M-4673-MONOMER.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
HAMAPi MF_00685. GlgB.
InterProi IPR006048. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view ]
PIRSFi PIRSF000463. GlgB. 1 hit.
SUPFAMi SSF51445. SSF51445. 1 hit.
TIGRFAMsi TIGR01515. branching_enzym. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGLGB_BACCQ
AccessioniPrimary (citable) accession number: B9J2G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: September 3, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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