GLGB_THEVB
ID GLGB_THEVB Reviewed; 766 AA.
AC Q8DLB8;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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}; OrderedLocusNames=tll0578;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC08130.1; -; Genomic_DNA.
DR RefSeq; NP_681368.1; NC_004113.1.
DR RefSeq; WP_011056426.1; NC_004113.1.
DR AlphaFoldDB; Q8DLB8; -.
DR SMR; Q8DLB8; -.
DR STRING; 197221.22294299; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; BAC08130; BAC08130; BAC08130.
DR KEGG; tel:tll0578; -.
DR PATRIC; fig|197221.4.peg.610; -.
DR eggNOG; COG0296; Bacteria.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000440; 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..766
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188754"
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 766 AA; 89885 MW; 42ED3BCF9036035E CRC64;
MTVSPEQIDR IVSNQHHDPF EILGCHQIQQ NGQSVWAVRA YLPNAERVSV LCPEQRQEYP
MTPVHHPHFF ECHIPVAELN NYQLKIYENG HERVIYDPYA FRSPKLTDFD IHLFAEGNHH
RIYEKLGAHL LTVDGVEGVY FAVWAPNARN VSVIGDFNHW DGRKHQMARR GNGIWELFIP
GLSVGERYKY EIKNQEGHIY EKSDPYGFYQ EPRPKTASIV TDLNSYEWGD SDWLEKRRHT
DPLNQPISVY EVHLGSWLHA SMEDPPIGAD GQPQEPVQAA ELKPWARFLT YRELAAKLIP
YVKELGYTHI ELLPVAEHPF DGSWGYQVTG YYAPTSRYGS PHDFMYFVDQ CHQNGIGVIV
DWVPGHFPKD GHGLAFFDGT HLYEHADPRK GEHKEWGTLV FNYGRHEVRN FLVANALFWF
DKYHIDGIRV DAVASMLYLD YGRKEGEWIP NEYGGRENLE AANFLRQVNH VIFSYFPGIL
SIAEESTAWP MVSWPTYMGG LGFNLKWNMG WMHDMLDYFS MDPWFRQFHH NNVTFSMWYH
HSENFMLALS HDEVVHGKSH IIGKMPGDRW QKFANLRCLF AYMFTHPGKK TMFMGMEFAQ
WSEWNVWSDL EWHLLQYEPH QQIKRFFGDL NHLYRSQPAL YSQDFKQEGF EWIDCSDNRH
SVVSFIRWDK DYQDFVVVVC NFTPQPHSHY RIGVPEHGFY RELFNSDARE YGGSNMGNLG
GKWADEWPYH QRRYSLDLCL PPLAVLILKL DREKTVAERA RYNLQS
