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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
 
 
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