GLGB_YEAST
ID GLGB_YEAST Reviewed; 704 AA.
AC P32775; D3DLN8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=1,4-alpha-glucan-branching enzyme;
DE EC=2.4.1.18;
DE AltName: Full=Glycogen-branching enzyme;
GN Name=GLC3; OrderedLocusNames=YEL011W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1634552; DOI=10.1016/s0021-9258(18)42169-2;
RA Thon V.J., Vigneron-Lesens C., Marianne-Pepin T., Montreuil J., Decq A.,
RA Rachez C., Ball S.G., Cannon J.F.;
RT "Coordinate regulation of glycogen metabolism in the yeast Saccharomyces
RT cerevisiae. Induction of glycogen branching enzyme.";
RL J. Biol. Chem. 267:15224-15228(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- DEVELOPMENTAL STAGE: Expressed during the transition between the late
CC exponential and stationary growth phases, coincident with maximal
CC glycogen accumulation.
CC -!- MISCELLANEOUS: Present with 1230 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; M76739; AAA34632.1; -; Genomic_DNA.
DR EMBL; U18530; AAB64488.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07642.1; -; Genomic_DNA.
DR PIR; S50448; S50448.
DR RefSeq; NP_010905.1; NM_001178826.1.
DR AlphaFoldDB; P32775; -.
DR SMR; P32775; -.
DR BioGRID; 36720; 20.
DR DIP; DIP-3873N; -.
DR IntAct; P32775; 10.
DR MINT; P32775; -.
DR STRING; 4932.YEL011W; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR iPTMnet; P32775; -.
DR MaxQB; P32775; -.
DR PaxDb; P32775; -.
DR PRIDE; P32775; -.
DR EnsemblFungi; YEL011W_mRNA; YEL011W; YEL011W.
DR GeneID; 856705; -.
DR KEGG; sce:YEL011W; -.
DR SGD; S000000737; GLC3.
DR VEuPathDB; FungiDB:YEL011W; -.
DR eggNOG; KOG0470; Eukaryota.
DR GeneTree; ENSGT00390000017040; -.
DR HOGENOM; CLU_011131_2_2_1; -.
DR InParanoid; P32775; -.
DR OMA; FGMKWMM; -.
DR BioCyc; YEAST:YEL011W-MON; -.
DR Reactome; R-SCE-3322077; Glycogen synthesis.
DR UniPathway; UPA00164; -.
DR PRO; PR:P32775; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32775; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IMP:SGD.
DR GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:SGD.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR43651; PTHR43651; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF02922; CBM_48; 1.
DR PIRSF; PIRSF000463; GlgB; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Glycogen biosynthesis; Glycosyltransferase; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..704
FT /note="1,4-alpha-glucan-branching enzyme"
FT /id="PRO_0000188786"
FT ACT_SITE 356
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 417
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 564
FT /note="S -> T (in Ref. 1; AAA34632)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 81116 MW; 9C227E107B825F27 CRC64;
MYNIPDNVKG AVEFDPWLKP FADVLSERRY LADKWLYDIT HATPDGSYQS LSKFARDSYK
SYGLHANPET KEITYKEWAP NAERAFLVGD FNNWDTTSHE LKNKDEFGNF TITLHPLPNG
DFAIPHDSKI KVMFILPDGS KIFRLPAWIT RATQPSKETS KQFGPAYEGR FWNPENPYKF
VHPRPKFSES VDSLRIYEAH VGISSPEPKI TTYKEFTEKV LPRIKYLGYD AIQLMAIMEH
AYYASFGYQV TNFFAASSRF GTPEELKELI DTAHSMGILV LLDVVHSHAS KNVEDGLNMF
DGSDHQYFHS ISSGRGEHPL WDSRLFNYGK FEVQRFLLAN LAFYVDVYQF DGFRFDGVTS
MLYVHHGVGA GGSFSGDYNE YLSRDRSFVD HEALAYLMLA NDLVHEMLPN LAVTVAEDVS
GYPTLCLPRS IGGTGFDYRL AMALPDMWIK LIKEKKDDEW EMGSIVYTLT NRRYGEKVVA
YCESHDQALV GDKTLAFWLM DAAMYTDMTV LKEPSIVIDR GIALHKMIRL ITHSLGGEAY
LNFEGNEFGH PEWLDFPNVN NGDSYKYARR QFNLADDPLL RYQNLNEFDR SMQLCEKRHK
WLNTKQAYVS LKHEGDKMIV FERNNLLFIF NFHPTNSYSD YRVGVEKAGT YHIVLNSDRA
EFGGHNRINE SSEFFTTDLE WNNRKNFLQV YIPSRVALVL ALKE