GLGB_SYNPW
ID GLGB_SYNPW Reviewed; 761 AA.
AC A5GJR7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
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};
GN OrderedLocusNames=SynWH7803_0756;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CT971583; CAK23182.1; -; Genomic_DNA.
DR RefSeq; WP_011932665.1; NC_009481.1.
DR AlphaFoldDB; A5GJR7; -.
DR SMR; A5GJR7; -.
DR STRING; 32051.SynWH7803_0756; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; A5GJR7; -.
DR EnsemblBacteria; CAK23182; CAK23182; SynWH7803_0756.
DR KEGG; syx:SynWH7803_0756; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_3; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001566; Chromosome.
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; -; 2.
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; 2.
DR PIRSF; PIRSF000463; GlgB; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
DR TIGRFAMs; TIGR01515; branching_enzym; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..761
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000045004"
FT ACT_SITE 431
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 484
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 761 AA; 88001 MW; BB022989B282244C CRC64;
MTNTVLEWMV EDAQRLAECR HDHPFAVLGP QPQEDGTWVL RAWMPEAEGV TLLLGDQEMG
MSTPHHPWIF EASVAHDPGC AYRLRVHRGG ITHEQHDPWA FRQDWMGEMD RHLFAEGNHH
HIWRRMGAHH CEREGIPGVM FCLWAPHARS VSVIGDLNSW DGRHHPMQQR LGGIWELFVP
GLAEGQLYKY EIRTQEGHCY QKADPYGFQH EVRPDTSSVV SHLDGFHWTD TDWIQKRDSS
NPLDQPIAVY EMHLGSWIHA AADEPFIEAD GTPRAPVPAA DLKPGARLLT YPELADRLIP
YVKERGFTHI ELMPITEHPF DGSWGYQVTG WYAPTSRYGT PDEFRAFVDR CHAEGIGVII
DWVPGHFPRD SHGLAFFDGC HLYEHADPRI GEHKEWGTLI FNYSRNEVRN FLVANLVFWF
DQFHIDGIRV DAVASMLYRD YLRPDGEWLP NEHGGRENTE AVQFLQQANH VLFQHFPGAL
SIAEESTTWP MVTQPTDIGG LGFNLKWNMG WMHDMLDYFE LDPWFRQFHQ NNITFSIWYT
YTENFMLALS HDEVVHGKSN LLHKMPGDDW QKYANTRALL AYMWTHPGKK TIFMGMEFGQ
RAEWNVWGDL QWDLLNYEPH QGVQRMVDDL NGLYKSEPAL WRDDFDQYGF QWIDCNDNRH
SVISFMRRES TSGTWLVVVA NFTPQSHSHY RVGVPLAGYY EEIFNTDASK YGGSNLGNMG
GKPTEEWGIH GYENSLDLCL PPLSLMVFKH DPKKSLNPVQ E