ID   GLGB_RHIRD              Reviewed;         734 AA.
AC   P52979;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   24-JAN-2024, entry version 112.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB;
DE            EC=2.4.1.18;
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase;
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme;
DE   AltName: Full=Glycogen branching enzyme;
DE            Short=BE;
GN   Name=glgB;
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A348;
RX   PubMed=9851999; DOI=10.1128/jb.180.24.6557-6564.1998;
RA   Ugalde J.E., Lepek V., Uttaro A.D., Estrella J., Iglesias A., Ugalde R.A.;
RT   "Gene organization and transcription analysis of the Agrobacterium
RT   tumefaciens glycogen (glg) operon: two transcripts for the single
RT   phosphoglucomutase gene.";
RL   J. Bacteriol. 180:6557-6564(1998).
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:0000250}.
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   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF033856; AAD03472.1; -; Genomic_DNA.
DR   AlphaFoldDB; P52979; -.
DR   SMR; P52979; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   eggNOG; COG0296; Bacteria.
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; 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..734
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000188671"
FT   ACT_SITE        417
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        470
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   734 AA;  83623 MW;  70A3CD35A77F31E6 CRC64;
     MKKPLNSAEE KKTGDITKAE IEAIKSGLHS NPFQIIPLHE TPEGFSARCF IPGAEEVSVL
     TLDGNFVGEL KQIDPDGFFE GRIDLSKRQP VRYRACRDDA EWAVTDPYSF GPVLGPMDDY
     FVREGSICGY STGWARIPLK LEGVEGFHFA VWAPNGRRVS VVGDFNNWDG RRHVMRFRKD
     TGIWEIFAPD VYACAYKFEI LGANGELLPL KADPYARRGE LRPKNASVTA PELTQKWEDQ
     AHREHWAQVD QRRQPISIYE VHAGSWQRSE DGTFLSWDEL EAQLIPYCTD MGFTHIEFLP
     ITEHPYDPSW GYQTTGLYAP TARFGDPEGF ARFVNGAHKV GIGVLLDWVP AHFPTDEHGL
     RWFDGTALYE HADPRQGFHP DWNTAIYNFG RIEVMSYLIN NALYWAEKFH LDGLRVDAVA
     SMLYLDYSRK EGEWIPNEYG GRENLESVRF LQKMNSLVYG THPGVMTIAE ESTSWPKVSQ
     PVHEGGLGFG FKWNMGFMHD TLSYFSREPV HRKFHHQELT FGLLYAFTEN FVLPLSHDEV
     VHGKGSLIAK MSGDDWQKFA NLRSYYGFMW GYPGKKLLFM GQEFAQWSEW SEKGSLDWNL
     RQYPMHEGMR RLVRDLNLTY RSKAALHARD CEPDGFRWLV VDDHENSVFA WLRTAPGEKP
     VAVICNLTPV YRENYYVPLG VAGRWREILN TDAEIYGGSG KGNGGRVQAV DAGGEIGAML
     VLPPLATIML EPEN
//