ID GLGB_RHOMR Reviewed; 621 AA. AC Q93HU3; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 13-SEP-2023, entry version 99. DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000255|HAMAP-Rule:MF_00685}; DE EC=2.4.1.18 {ECO:0000255|HAMAP-Rule:MF_00685}; DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000255|HAMAP-Rule:MF_00685}; DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685}; DE AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685}; DE Short=BE {ECO:0000255|HAMAP-Rule:MF_00685}; GN Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685}; OS Rhodothermus marinus (Rhodothermus obamensis). OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae; OC Rhodothermus. OX NCBI_TaxID=29549; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11778874; DOI=10.1007/s00253-001-0841-3; RA Shinohara M.L., Ihara M., Abo M., Hashida M., Takagi S., Beck T.C.; RT "A novel thermostable branching enzyme from an extremely thermophilic RT bacterial species, Rhodothermus obamensis."; RL Appl. Microbiol. Biotechnol. 57:653-659(2001). CC -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages CC in glycogen by scission of a 1,4-alpha-linked oligosaccharide from CC growing alpha-1,4-glucan chains and the subsequent attachment of the CC oligosaccharide to the alpha-1,6 position. {ECO:0000255|HAMAP- CC Rule:MF_00685}. 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00685}; CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00685}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00685}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00685}. 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; AB060080; BAB69858.1; -; Genomic_DNA. DR PDB; 6JOY; X-ray; 2.39 A; A=1-621. DR PDBsum; 6JOY; -. DR AlphaFoldDB; Q93HU3; -. DR SMR; Q93HU3; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR BRENDA; 2.4.1.18; 5425. DR UniPathway; UPA00164; -. DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-UniRule. 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-UniRule. DR CDD; cd11322; AmyAc_Glg_BE; 1. DR CDD; cd02855; E_set_GBE_prok_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 HAMAP; MF_00685; GlgB; 1. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR037439; Branching_enzy. DR InterPro; IPR006407; GlgB. DR InterPro; IPR044143; GlgB_N_E_set_prok. 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 NCBIfam; TIGR01515; branching_enzym; 1. 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; Carbohydrate metabolism; Glycogen biosynthesis; KW Glycogen metabolism; Glycosyltransferase; Transferase. FT CHAIN 1..621 FT /note="1,4-alpha-glucan branching enzyme GlgB" FT /id="PRO_0000188737" FT ACT_SITE 305 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" FT ACT_SITE 356 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685" FT HELIX 6..13 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 24..28 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 30..38 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 43..49 FT /evidence="ECO:0007829|PDB:6JOY" FT TURN 50..53 FT /evidence="ECO:0007829|PDB:6JOY" FT TURN 56..58 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 68..74 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 81..88 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 91..95 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 103..112 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 114..117 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 128..133 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 145..149 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 156..160 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 165..179 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 182..187 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 215..227 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 231..236 FT /evidence="ECO:0007829|PDB:6JOY" FT TURN 245..248 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 249..258 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 280..296 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 301..304 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 307..311 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 316..320 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 331..347 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 352..355 FT /evidence="ECO:0007829|PDB:6JOY" FT TURN 362..365 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 368..370 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 376..379 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 381..392 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 395..401 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 402..406 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 408..411 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 417..421 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 423..426 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 433..436 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 441..457 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 458..465 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 468..470 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 484..488 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 490..508 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 510..512 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 517..519 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 520..524 FT /evidence="ECO:0007829|PDB:6JOY" FT TURN 528..531 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 532..538 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 543..549 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 551..553 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 555..564 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 566..573 FT /evidence="ECO:0007829|PDB:6JOY" FT HELIX 577..579 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 593..595 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 600..608 FT /evidence="ECO:0007829|PDB:6JOY" FT STRAND 613..618 FT /evidence="ECO:0007829|PDB:6JOY" SQ SEQUENCE 621 AA; 72238 MW; 1F93D30FFB29697A CRC64; MSWLTEEDIR RWESGTFYDS YRKLGAHPDD EGTWFCVWAP HADGVSVLGA FNDWNPEANP LERYGGGLWA GYVPGARPGH TYKYRIRHGF YQADKTDPYA FAMEPPTGSP IEGLASIITR LDYTWHDDEW MRRRKGPASL YEPVSIYEVH LGSWRHKRPG ESFSYREIAE PLADYVQEMG FTHVELLPVM EHPYYGSWGY QVVGYYAPTF RYGSPQDLMY LIDYLHQRGI GVILDWVPSH FAADPQGLVF FDGTTLFEYD DPKMRYHPDW GTYVFDYNKP GVRNFLISNA LFWLEKYHVD GLRVDAVASM LYRDYSRKEW TPNIFGGREN LEAIDFIKKF NETVYLHFPE AMTIAEESTA WPGVSAPTYN NGLGFLYKWN MGWMHDTLDY IQRDPIYRKY HHDELTFSLW YAFSEHYVLP LSHDEVVHGK GSLWGKMPGD DWQKAANLRL LFGHMWGHPG KKLLFMGGEF GQHHEWNHDT QLEWHLLDQP YHRGIQLWVC DLNHLYRTNP ALWHDGPEGF EWIDFSDRDQ SVICYLRKNA GRMLLFVLNF TPVPREHYRV GVPIGGPWHE VLNSDAVAYG GSGMGNFGRV EAVPESWHGR PFHLELTLPP LAALILEPEH G //