ID   GLGB_BRASO              Reviewed;         712 AA.
AC   A4Z005;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   04-NOV-2026, 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=BRADO5817;
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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; CU234118; CAL79481.1; -; Genomic_DNA.
DR   RefSeq; WP_012029384.1; NC_009445.1.
DR   AlphaFoldDB; A4Z005; -.
DR   SMR; A4Z005; -.
DR   STRING; 114615.BRADO5817; -.
DR   KEGG; bra:BRADO5817; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_5; -.
DR   OMA; AADNTPW; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-UniRule.
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   FunFam; 2.60.40.10:FF:000169; 1,4-alpha-glucan branching enzyme GlgB; 1.
DR   FunFam; 2.60.40.1180:FF:000002; 1,4-alpha-glucan branching enzyme GlgB; 1.
DR   FunFam; 3.20.20.80:FF:000003; 1,4-alpha-glucan branching enzyme GlgB; 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; 2.
DR   HAMAP; MF_00685; GlgB; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR037439; Branching_enzy.
DR   InterPro; IPR006047; GH13_cat_dom.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR006407; GlgB.
DR   InterPro; IPR054169; GlgB_N.
DR   InterPro; IPR044143; GlgB_N_E_set_prok.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   NCBIfam; TIGR01515; branching_enzym; 1.
DR   NCBIfam; NF003811; glgB; 1.
DR   NCBIfam; NF008967; glgB; 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   Pfam; PF22019; GlgB_N; 1.
DR   PIRSF; PIRSF000463; GlgB; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 2.
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..712
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_1000061988"
FT   ACT_SITE        397
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        450
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   712 AA;  81178 MW;  2C98C9B7DC94AAA2 CRC64;
     MTHLSPEAFA IIEGRHADPF RYLGQHNVDG QTIVRAFLPE ASRVEVVGEH GEVAPLARIH
     DAGLFTGTMS SMQRYRLRAT FGDSVTDLED PYRFLPILGD FDLHLLGEGN HERLYDKLGA
     HPMVIDGVDG VGFVVLAPNA RRVSVVGDFN FWNARRHPMR VRGNGYWELF IPRARAGDHY
     KFDIIGPQGE HLPLKSDPMA FAAEMRPKTA SIVVDETRLP RPRPAPHDIN KLNKPVSIYE
     VHLGSWRRKD NNQWLTYREL AEQLPAYARD MGFTHIEFLP INEHPFDGSW GYQPTGLYAP
     TSRFGSPEDF CALVDACHRE GLAVWLDWVP GHFPDDPHGL GHFDGTALYE HANPMQGRHL
     DWGTLIYNYG RTEVANFLRS NALFWLERYG IDGLRVDAVA SMLYLDYSRP SGGWIPNKYG
     GRENLEAIEF LRRTNIDVFG HFPQATTAAE ESTAWPQVSR PVDTGGLGFG YKWNMGWMHD
     TLRYVSKDPI HRKYHHGEIL FGLHYAFSEN FILPLSHDEV VHGKRSILGR MPGDDWQRFA
     NLRAYYSFMF GHPGKKLLFM GCELAQEREW NHDTSLDWHL LGDARYAGIQ ALIRDLNHLY
     RNQPALHERD CDPEGFEWLI TDDADRNVFA WVRKGFDERA HCVVVVNFSP NVYYNYRVRA
     PLGGTWREVF NSDSSHYGGS NVGNVGQVHA SEDQHLNLIL PPMAAVFLVP EA
//