GLGB1_STRAW
ID GLGB1_STRAW Reviewed; 838 AA.
AC Q82JF0;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme 1 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme 1 {ECO:0000255|HAMAP-Rule:MF_00685};
DE Short=BE 1 {ECO:0000255|HAMAP-Rule:MF_00685};
GN Name=glgB1 {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=SAV_2805;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000030; BAC70516.1; -; Genomic_DNA.
DR AlphaFoldDB; Q82JF0; -.
DR SMR; Q82JF0; -.
DR STRING; 227882.SAV_2805; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; BAC70516; BAC70516; SAVERM_2805.
DR KEGG; sma:SAVERM_2805; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_11; -.
DR OMA; MNWPEIE; -.
DR BRENDA; 2.4.1.18; 5980.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000428; 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; 1.
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..838
FT /note="1,4-alpha-glucan branching enzyme GlgB 1"
FT /id="PRO_0000188747"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 513
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 566
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 838 AA; 92740 MW; 3BFDF6B6AD3869CE CRC64;
MIPRPPSDDR ANQNGDGSKK TGAKKTGAKK AAAAKKTAGK KATPAAKATA AKGAVTKKTG
KGKATAKKAV ADKAAAKATV PQQAVPKQAV SKRAVSKKAV PRKAVVKAAL DIPEAPVSPA
VAPDDRDRLL SGTHHAPHSV LGAHPVPGGV AFRVLRPYAL SVTVVTDDLR TELHDDGAGF
FTGLLPLRAV PDYRLHVAYE GTVHETEDAY RFLPALGELD LHLINEGRHE ELWTALGAEP
MTHQGVPGTR FTVWAPNARG VRLAGTFNFW DATAFPLRSL GSSGVWELFV PGVGEGELYK
FEITRPDGSK TLRADPVARR TEAPPRTSSI VHASHYAWAD EAWMAARGER PVHESPFSVY
EVHLPSWRPG LTYRQLAEQL PAYVADLGFT HVELLPVAEH PFGGSWGYQV TGFYAPTARL
GTPDDFKYLV DALHRAGVGV LMDWVPAHFP RDDWALAEFD GRPLYEHEDP LRAAHPDWGT
LEFDYGRREV RNFLVANAVY WCEEFHIDGL RVDAVASMLY LDYSREEGQW SPNEFGGREN
LDAVAFLQEM NATVYRRVPG VVTIAEESTA WEGVTRATHD NGLGFGLKWN MGWMHDSLGY
VQHEPVHRRF HHHEMTFSMV YAYSENYVLP ISHDEVVHGK GSLVSKMPGD WWQQRATERA
YLGFMWAHPG KQLLFMGQEF AQGAEWSETH GPDWWLLDPA YGAEPDHRGM RDLVRDLNTV
YRHEPALWER DTDPSGFAWV TGDAVEDNVF AFLRHAADGT PLLAVSNFSP VVRHDYRLGV
PDDIPAWHET LNTDGARYGG SDVTNPHPVK PEPQGRHGRP ASIRLTLPPL STLWLRPA
