1,4-alpha-glucan-branching enzyme - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32775 (GLGB_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
1,4-alpha-glucan-branching enzyme
EC=2.4.1.18

Alternative name(s):
Glycogen-branching enzyme

Gene names

Name:	GLC3
Ordered Locus Names:	YEL011W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	704 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
Pathway	Glycan biosynthesis; glycogen biosynthesis.
Developmental stage	Expressed during the transition between the late exponential and stationary growth phases, coincident with maximal glycogen accumulation.
Miscellaneous	Present with 1230 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.

Ontologies

Keywords
Biological process	Glycogen biosynthesis
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycogen biosynthetic process Inferred from mutant phenotype PubMed 1729600. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 14562095 PubMed 22842922. Source: SGD
Molecular_function	1,4-alpha-glucan branching enzyme activity Inferred from genetic interaction PubMed 1729600. Source: SGD cation binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 704

704

1,4-alpha-glucan-branching enzyme

PRO_0000188786

Sites

Active site

356

Nucleophile By similarity

Active site

417

Proton donor By similarity

Amino acid modifications

Modified residue

190

Phosphoserine Ref.5

Experimental info

Sequence conflict

564

S → T in AAA34632. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P32775 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 9C227E107B825F27
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FASTA

704

81,116

        10         20         30         40         50         60 
MYNIPDNVKG AVEFDPWLKP FADVLSERRY LADKWLYDIT HATPDGSYQS LSKFARDSYK 

        70         80         90        100        110        120 
SYGLHANPET KEITYKEWAP NAERAFLVGD FNNWDTTSHE LKNKDEFGNF TITLHPLPNG 

       130        140        150        160        170        180 
DFAIPHDSKI KVMFILPDGS KIFRLPAWIT RATQPSKETS KQFGPAYEGR FWNPENPYKF 

       190        200        210        220        230        240 
VHPRPKFSES VDSLRIYEAH VGISSPEPKI TTYKEFTEKV LPRIKYLGYD AIQLMAIMEH 

       250        260        270        280        290        300 
AYYASFGYQV TNFFAASSRF GTPEELKELI DTAHSMGILV LLDVVHSHAS KNVEDGLNMF 

       310        320        330        340        350        360 
DGSDHQYFHS ISSGRGEHPL WDSRLFNYGK FEVQRFLLAN LAFYVDVYQF DGFRFDGVTS 

       370        380        390        400        410        420 
MLYVHHGVGA GGSFSGDYNE YLSRDRSFVD HEALAYLMLA NDLVHEMLPN LAVTVAEDVS 

       430        440        450        460        470        480 
GYPTLCLPRS IGGTGFDYRL AMALPDMWIK LIKEKKDDEW EMGSIVYTLT NRRYGEKVVA 

       490        500        510        520        530        540 
YCESHDQALV GDKTLAFWLM DAAMYTDMTV LKEPSIVIDR GIALHKMIRL ITHSLGGEAY 

       550        560        570        580        590        600 
LNFEGNEFGH PEWLDFPNVN NGDSYKYARR QFNLADDPLL RYQNLNEFDR SMQLCEKRHK 

       610        620        630        640        650        660 
WLNTKQAYVS LKHEGDKMIV FERNNLLFIF NFHPTNSYSD YRVGVEKAGT YHIVLNSDRA 

       670        680        690        700 
EFGGHNRINE SSEFFTTDLE WNNRKNFLQV YIPSRVALVL ALKE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Coordinate regulation of glycogen metabolism in the yeast Saccharomyces cerevisiae. Induction of glycogen branching enzyme." Thon V.J., Vigneron-Lesens C., Marianne-Pepin T., Montreuil J., Decq A., Rachez C., Ball S.G., Cannon J.F. J. Biol. Chem. 267:15224-15228(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M76739 Genomic DNA. Translation: AAA34632.1. U18530 Genomic DNA. Translation: AAB64488.1. BK006939 Genomic DNA. Translation: DAA07642.1.
PIR	S50448.
RefSeq	NP_010905.1. NM_001178826.1.
3D structure databases
ProteinModelPortal	P32775.
SMR	P32775. Positions 197-361.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3873N.
IntAct	P32775. 10 interactions.
MINT	MINT-573503.
STRING	4932.YEL011W.
Protein family/group databases
CAZy	CBM48. Carbohydrate-Binding Module Family 48. GH13. Glycoside Hydrolase Family 13.
Proteomic databases
PaxDb	P32775.
PeptideAtlas	P32775.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YEL011W; YEL011W; YEL011W.
GeneID	856705.
KEGG	sce:YEL011W.
Organism-specific databases
CYGD	YEL011w.
SGD	S000000737. GLC3.
Phylogenomic databases
eggNOG	COG0296.
GeneTree	ENSGT00390000017040.
HOGENOM	HOG000175159.
KO	K00700.
OMA	ALYWFKE.
OrthoDB	EOG47M562.
Enzyme and pathway databases
UniPathway	UPA00164.
Gene expression databases
Genevestigator	P32775.
GermOnline	YEL011W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.60.40.10. 1 hit. 2.60.40.1180. 1 hit. 3.20.20.80. 1 hit.
InterPro	IPR006407. 1-4-A-glucan_branch_enz. IPR006048. A-amylase_b_C. 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]
PANTHER	PTHR10357. PTHR10357. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF02806. Alpha-amylase_C. 1 hit. PF02922. CBM_48. 1 hit. [Graphical view]
PIRSF	PIRSF000463. GlgB. 1 hit.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit. SSF81296. Ig_E-set. 1 hit.
ProtoNet	Search...
Other
NextBio	982774.

Entry information

Entry name

GLGB_YEAST

Accession

Primary (citable) accession number: P32775
Secondary accession number(s): D3DLN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program