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 27-MAR-2024, entry version 112. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR382129; CAG81834.1; -; Genomic_DNA. DR RefSeq; XP_501531.1; XM_501531.1. DR AlphaFoldDB; Q6CCT1; -. DR SMR; Q6CCT1; -. DR STRING; 284591.Q6CCT1; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. 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; YEMHLGS; -. DR OrthoDB; 96at2759; -. 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:0005978; P:glycogen biosynthetic process; IBA:GO_Central. DR CDD; cd11321; AmyAc_bac_euk_BE; 1. DR CDD; cd02854; E_set_GBE_euk_N; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1. DR PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 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; (Trans)glycosidases; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 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 //