ID   GLGB_YARLI              Reviewed;         691 AA.
AC   Q6CCT1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=YALI0C06798g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR382129; CAG81834.1; -; Genomic_DNA.
DR   RefSeq; XP_501531.1; XM_501531.1.
DR   AlphaFoldDB; Q6CCT1; -.
DR   SMR; Q6CCT1; -.
DR   STRING; 4952.CAG81834; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q6CCT1; -.
DR   EnsemblFungi; CAG81834; CAG81834; YALI0_C06798g.
DR   GeneID; 2909223; -.
DR   KEGG; yli:YALI0C06798g; -.
DR   VEuPathDB; FungiDB:YALI0_C06798g; -.
DR   HOGENOM; CLU_011131_2_2_1; -.
DR   InParanoid; Q6CCT1; -.
DR   OMA; FGMKWMM; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001300; Chromosome C.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
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; IBA:GO_Central.
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   3: Inferred from homology;
KW   Glycogen biosynthesis; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..691
FT                   /note="1,4-alpha-glucan-branching enzyme"
FT                   /id="PRO_0000188785"
FT   ACT_SITE        333
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        398
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   691 AA;  79306 MW;  24D19060CFAB35C2 CRC64;
     MTLQVCKDDP WLKPFEEELL RRQALVGQWK DHFAKEGGLA EFAASYKRYG LHVNKDNSVT
     YREWAPGASE AVLTGDFNGW DRQQYHMTRD EYGLWSVTVP PTSDGQVAIP HNSKVKLALK
     TSNGQWVDRL PAWSTYVVQD LSKSPIYEAV FWNPPESEKY QWKNKSPPTP ANAQIYEAHV
     GISSSEPRVG TYKEFTKNIL PRIHKLGYNV IQLMAIMEHA YYASFGYQVT SFYAISSRYG
     TPEDLKELID TAHGMGITVL LDVVHSHACK NVDDGLNNFD GTDHQYFHGG AKGDHPQWDS
     KLFDYGKYEV LRFLLSNLRF YIEEYHFDGF RFDGVTSMLY KHHGLGTGFS GGYHEYFGDE
     HVDQQAVVYL MLAHELMREL QPLLRPGEDA GNFLSIAEDV SGMPALCRPV SEGGVGFDYR
     LAMAIPDMWI KLVKETRDED WDMGNIVFTL TNRRHREKTI AYAESHDQAL VGDKTLAFWL
     MDKEMYTSMS VLSDPNPIID RGIALHKMIR LITHSLGGEG YLNFEGNEFG HPEWLDFPRE
     GNGSSFHYCR RQWPVVDDKL LRYQHLNEFD AAMQHRGDHY GWLSADQAYV SLKNEDDKVV
     VYERAGLVFV FNFHPNKSFT DYRIGVDQPG TYTLVLDSDS PEFGGFGRID HEKTRCHTEP
     LEWNGRANCM HIYIPSRVAL VFAREDDPRR K