ID GLGB_CANGA Reviewed; 706 AA. AC Q6FJV0; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 120. 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=CAGL0M03377g; OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces. OX NCBI_TaxID=284593; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS RC 138; 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; CR380959; CAG62470.1; -; Genomic_DNA. DR RefSeq; XP_449494.1; XM_449494.1. DR PDB; 7P43; X-ray; 1.93 A; A/B=1-706. DR PDB; 7P44; X-ray; 2.40 A; A/B=1-706. DR PDB; 7P45; X-ray; 2.09 A; A=1-706. DR PDBsum; 7P43; -. DR PDBsum; 7P44; -. DR PDBsum; 7P45; -. DR AlphaFoldDB; Q6FJV0; -. DR SMR; Q6FJV0; -. DR STRING; 284593.Q6FJV0; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblFungi; CAGL0M03377g-T; CAGL0M03377g-T-p1; CAGL0M03377g. DR GeneID; 2891502; -. DR KEGG; cgr:CAGL0M03377g; -. DR CGD; CAL0136349; CAGL0M03377g. DR VEuPathDB; FungiDB:B1J91_M03377g; -. DR VEuPathDB; FungiDB:CAGL0M03377g; -. DR eggNOG; KOG0470; Eukaryota. DR HOGENOM; CLU_011131_2_2_1; -. DR InParanoid; Q6FJV0; -. DR OMA; YEMHLGS; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000002428; Chromosome M. DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD. DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC. 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; IEA:UniProtKB-UniPathway. 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 1: Evidence at protein level; KW 3D-structure; Glycogen biosynthesis; Glycosyltransferase; KW Reference proteome; Transferase. FT CHAIN 1..706 FT /note="1,4-alpha-glucan-branching enzyme" FT /id="PRO_0000188779" FT ACT_SITE 358 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 419 FT /note="Proton donor" FT /evidence="ECO:0000250" FT HELIX 8..10 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 11..16 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 18..23 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 24..42 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 53..63 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 64..68 FT /evidence="ECO:0007829|PDB:7P43" FT TURN 70..72 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 85..91 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:7P45" FT STRAND 110..116 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 131..137 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 143..146 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 159..165 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:7P43" FT TURN 191..193 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 207..211 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 215..221 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 223..229 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 232..238 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 253..258 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 260..262 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 265..277 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 281..286 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 295..299 FT /evidence="ECO:0007829|PDB:7P43" FT TURN 300..303 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 304..310 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 313..315 FT /evidence="ECO:0007829|PDB:7P45" FT TURN 321..323 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 333..349 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 354..357 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 360..364 FT /evidence="ECO:0007829|PDB:7P43" FT TURN 366..369 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 371..374 FT /evidence="ECO:0007829|PDB:7P44" FT HELIX 380..384 FT /evidence="ECO:0007829|PDB:7P43" FT TURN 386..388 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 393..409 FT /evidence="ECO:0007829|PDB:7P43" FT TURN 411..413 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 415..418 FT /evidence="ECO:0007829|PDB:7P43" FT TURN 425..428 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 431..433 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 439..442 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 446..456 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 459..461 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 464..472 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 487..490 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 497..502 FT /evidence="ECO:0007829|PDB:7P43" FT TURN 507..509 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 511..514 FT /evidence="ECO:0007829|PDB:7P45" FT HELIX 518..537 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 540..545 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 548..550 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 561..563 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 575..578 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 584..600 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 604..606 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 610..615 FT /evidence="ECO:0007829|PDB:7P43" FT TURN 616..619 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 620..625 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 628..633 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 640..649 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 651..658 FT /evidence="ECO:0007829|PDB:7P43" FT HELIX 662..664 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 679..681 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 686..694 FT /evidence="ECO:0007829|PDB:7P43" FT STRAND 698..704 FT /evidence="ECO:0007829|PDB:7P43" SQ SEQUENCE 706 AA; 81044 MW; 18872CAADBCD2A87 CRC64; MSLTKIPENV QGAVSIDPWL EPFADVLSER RYLADKWLYD IKHATPDGSE QSLVDFARNA YKTYGLHANQ QTKEIVYREW APNAQRAFLV GEFNNWNEES HEMKHKDEFG VFSITLAPLE NGDFAIPHDS KIKVMFVLPD GSKVYRIPAW ITRATQPSKE TAQKYGPTYE GRFWNPPNSY QFKHQRPKFN LANDSIKIYE AHIGISSPEP KVASYKEFTQ NVLPRIKHLG YDAIQLMAIM EHAYYASFGY QVTNFFAISS RYGTPEDLKE LIDTAHSMGI LVLLDVIHSH ASKNSEDGLN MFDGSDHQYF HSLTSGRGEH PLWDSRLFNY GSFEVQRFLL ANLAYYIDVY QFDGFRFDGV TSMLYLHHGV GAGGAFSGDY NEYLSRDRSG VDHEALAYLM LANDLVHDLL PESAVTIAED VSGYPTLCLP RTAGGGGFDY RLAMALPDMW IKLLKTKQDD DWDMGHIVHT LTNRRHGEKV VAYCESHDQA LVGDKTLAFW LMDAAMYTDM TVLKEPTLVI DRGIALHKMI RLITHSLGGE AYLNFEGNEF GHPEWLDFPR VGNNDSYHYA RRQFNLVDDD LLRYRHLNEF DAAMQNCESK HQWLNTPQAY VSLKHEVDKV IAFERNGHLF VFNFHPTQSF TDYRIGVDVA GTYKIVLNTD RAEFGGHNRI DEAQEFFTTD LEWNNRRNFI QVYIPSRTAI VLTRQM //