GLGB_RHOMR
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 25-MAY-2022, entry version 95.
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; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; 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}.
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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; cd02855; E_set_GBE_prok_N; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 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 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.
DR TIGRFAMs; TIGR01515; branching_enzym; 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
