GLGB_SYNR3
ID GLGB_SYNR3 Reviewed; 772 AA.
AC A5GSG4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=SynRCC307_0920;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
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; CT978603; CAK27823.1; -; Genomic_DNA.
DR RefSeq; WP_011935337.1; NC_009482.1.
DR AlphaFoldDB; A5GSG4; -.
DR SMR; A5GSG4; -.
DR STRING; 316278.SynRCC307_0920; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; CAK27823; CAK27823; SynRCC307_0920.
DR KEGG; syr:SynRCC307_0920; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_3; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001115; 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; 1.
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..772
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000045005"
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 772 AA; 88398 MW; 260B2C49D9B62588 CRC64;
MALATLDWMS KDAERLAQCN HDHPQAVLGP QQLEDGRWVV RVWMPEASRV VLLHQGHEHA
LENPHHAWIF EGELSSNPGS QYRLRVERAG ITHEQHDPYA FRQEWMGAMD RHLFAEGNHH
HIWQRMGAHP HLQDGVAGVQ FCLWAPNARS VSVIGDCTNW DGRHLPMQQR IGGIWELFVP
GLGAGAHYKY EIHTQQGHCY EKADPYGFQH EVRPAQASVV ASLKGYQWGD DAWLKQRDNR
NPLEQPVSVY EMHMGSWMHG SWDEPYIEAD GTPRAPVPAA DLKPGARLLT YPELADRVIP
YVKARGFTHI ELMPMAEHPF DGSWGYQVTG FYAPTSRFGT LDEFRAFVDR CHAEGIGVIL
DWVPGHFPKD AHGLAFFDGS HLYEHGDPRI GEHKEWGTLI FNYSRNEVRN FLVANLVFWF
EELHIDGIRV DAVASMLYRD YLRPDGEWIA NEHGGRENLE AVRFLQQANS VLFHYFPGAL
SIAEESTTWP LVTMPTSMGG LGFNLKWNMG WMHDMLDYFE LDHWFRQFHQ NNITFSIWYA
HTENFMLALS HDEVVHGKSH LLHKMPGSDE LKFANVRALL TYMWTHPGKK TIFMGMEFAQ
RGEWNVWGDL EWDKLQFPEH QGVVNLVDDL NALYKSEPAL WRNDFDSFGF QWIDCDDTNH
SVVSFMRRDE KEGNWVVVVC NFTPEGHGNY RIGVPVDGFY TELFNSDGAR YGGSNQGNLG
GKFSDDWGMH SYGQSLDLCL PPLTVMVFKH DPNRQREAAK DEAAAKLGGS LG
