GLGB_SYNS9
ID GLGB_SYNS9 Reviewed; 764 AA.
AC Q3AYE2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 113.
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=Syncc9902_0919;
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) 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; CP000097; ABB25885.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3AYE2; -.
DR SMR; Q3AYE2; -.
DR STRING; 316279.Syncc9902_0919; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q3AYE2; -.
DR EnsemblBacteria; ABB25885; ABB25885; Syncc9902_0919.
DR KEGG; sye:Syncc9902_0919; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_3; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002712; 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..764
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260707"
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 764 AA; 87685 MW; F22CD98EEF60DBA7 CRC64;
MGGAAVLDWM VQDGVRLENC RHDHPLAVLG PQPDDQGWTV RVWMPEAQKV TLLLGSQEIV
TSTPNHPWIF EASTPSDPGS NYKLRVERGG ITTEQHDPWA FRHEWMGEMD RHLFAEGNHH
HIWQRMGAHL TQIDGISGVM FCLWAPNALT ASVLGDLNSW DGRHHPMQKR LGGIWELFVP
GLDAGTLYKY EIRSQEGHCY QKADPYGFQH EVRPDNSSVV ARLEGYSWSD SSWMQDRDSR
NALDQPISVY EMHIGSWIHA SADEPWIQPD GQPRAPVPAA DMKPGARLLT YAELSDRLIP
YVKERGFTHI ELMPITEHPF DGSWGYQVTG WYAPTSRYGT PDEFRAFVDR CHAEGIGVII
DWVPGHFPKD AHGLAFFDGT HLYEHGDPRI GEHKEWGTLI FNYSRNEVRN FLVANLVFWF
EQFHIDGIRV DAVASMLYRD YLRPDGEWLP NENGGRENTE AVRFLQQANH VLFQHYPGAL
SIAEESTTWP MVTQPTDMGG LGFNLKWNMG WMHDMLDYFE LDPWFRQFHQ NNITFSIWYT
YTENFMLALS HDEVVHGKSH LLHKMPGDDW QKYANTRALL AYMWTHPGKK TIFMGMEFGQ
RAEWNVWGDL EWDLLNYEPH KGIQRLVDDL NVLYKAQPAL WRDDFDQFGF QWIDCNDNRH
SVISFMRRDS ASGTWLVVVA NFTPQSHANY RVGVPLEGFY EEIFNTDAAK YGGSNLGNMG
GKPTDACGIH GYEHSLDLCL PPLSLVVFQH DPKRTLIESS APSD
