ID   GLGB_SHESM              Reviewed;         745 AA.
AC   Q0HGI8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=Shewmr4_2758;
OS   Shewanella sp. (strain MR-4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. MR-4.";
RL   Submitted (AUG-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; CP000446; ABI39829.1; -; Genomic_DNA.
DR   RefSeq; WP_011623509.1; NC_008321.1.
DR   AlphaFoldDB; Q0HGI8; -.
DR   SMR; Q0HGI8; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; she:Shewmr4_2758; -.
DR   HOGENOM; CLU_004245_3_2_6; -.
DR   UniPathway; UPA00164; -.
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; cd11322; AmyAc_Glg_BE; 1.
DR   CDD; cd02855; E_set_GBE_prok_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   NCBIfam; TIGR01515; branching_enzym; 1.
DR   PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..745
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000260699"
FT   ACT_SITE        416
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        469
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   745 AA;  85107 MW;  7FDD90AA5A188EFA CRC64;
     MMTQAQTYFY DGSDVALLNG QYTDVFSLLG MHSINEGKAL VVRCFLRNAQ KVDVISLKDG
     RKVASLERVN EAGLFAGTLG RRVKPFLYAL RVVYPLCELD IIDPYQFGSL LDSQDLYLFG
     EGSSEQAYRF LGANWRQVDS VEGVHFCVWA PNAKRVSVVG DFNHWDDTRH VMRQHMANGL
     WEIFLPDVAE GTHYKFDLVY QNGERHAKSD PMATQMECAP HNASIVPKKH QHPWADTQWM
     HKRATTAWHR AAMSIYEVQL GSWRRKGEFG EQYFDYQDLI EQLIPYVKEQ GFTHIELMPV
     SEYPFDGSWG YQPVGLYAPT HRFGDANGLK AFIDACHQAE IGVLLDWVAA HFPKDPHGLV
     RFDGTCLYEH EDPRKGTHPD WDTLIYNYDR GEVRSFLLSN ACYWLREFHL DGLRLDAVSS
     MLYLDYSREP GQWLPNAYGG RENLEAIHFL QMLNQRLYQA FPGICMIAEE STAFAGVTKP
     TDSGGLGFGF KWNMGWMNDS LSYLGRDPIY RQYHHNQLTF SLMYAYSEQF MLSISHDEVV
     HGKGSLLHKI PGDDWQKFAT LKAYYGFMWG HPGKKLLFMG SEFAQRDEWN HNHSLDWHLL
     AFEPHQGVQR WLRDLNQLYR QFPALSVLDY ESQGFRWLDC DNGRDSIFSF VRYGEGSDVP
     LVFVVNMTPT LHQGFRIGLP QGGDFCEYLN SDSHLYGGSN QGNAGKVIAE DLPWQGMASS
     ALITVPPLGC LILGPATDAP RDTSL
//