ID   GLGB2_RHIJ3             Reviewed;         736 AA.
AC   Q1M3A7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Glycogen branching enzyme 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE            Short=BE 2 {ECO:0000255|HAMAP-Rule:MF_00685};
GN   Name=glgB2 {ECO:0000255|HAMAP-Rule:MF_00685};
GN   OrderedLocusNames=pRL120710;
OS   Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium
OS   leguminosarum bv. viciae).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium;
OC   Rhizobium johnstonii.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 114642 / LMG 32736 / 3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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; AM236086; CAK12419.1; -; Genomic_DNA.
DR   RefSeq; WP_011649463.1; NC_008378.1.
DR   AlphaFoldDB; Q1M3A7; -.
DR   SMR; Q1M3A7; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; CAK12419; CAK12419; pRL120710.
DR   KEGG; rle:pRL120710; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_5; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000006575; Plasmid pRL12.
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..736
FT                   /note="1,4-alpha-glucan branching enzyme GlgB 2"
FT                   /id="PRO_0000260685"
FT   ACT_SITE        415
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        468
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   736 AA;  81853 MW;  F81E22D2BE2DA1CA CRC64;
     MNVERSELLA GIGQDALWAL IEGRHGDPFS ILGPHQSGGM TIVRVYLPGA EAVDLIDATS
     GRVVAPFSIA HPSGLFAATV ASRTGYRLRI TWPDAVQITE DPYSFGLLLG ELDLHLISEG
     THYSLSRTLG AVAMSIDGIS GVRFAVWAPN ARRVSVVGDF NAWDGRRNPM RLRPSAGVWE
     LFIPRLAPGE RYKFEIVDAE GTCLPQKADP VARASEAAPS TASIVASSTP FRWTDDGWMK
     GRSRQDRLEG AFSVYEVHVG SWLRDQKDGN RSLDWVELSQ RLVPYVSDMG FTHIELLPIM
     EHPFGGSWGY QPLGLFAPTG RYGTPEDFAY FVDRCHGAGL GVILDWVPAH FPTDVWGLAR
     FDGSALYEHE DPREGFHRDW NTLIYNLGRN EVKGFLIASA LEWLERYHID GLRVDAVASM
     LYRDYSRNEG EWIPNQYGGR ENLEAVEFFK HLNSIIHERC PHAMTIAEES TAWPGVTKPP
     EQGGLGFDIK WNMGWMHDSL SYIEKDPIYR SYAHGTMTFG MIYAYSERFI LPISHDEVVY
     GKGSLLTKMP GDEWQKFANL RSYLAFMWGH PGKKLLFMGS EIAQPSEWNH DGSVTWDVLD
     QPQHVGIQRL VKDLNGLYGD EPALQFGDFH SEGFEWAAAD DAVNSVLGML RYAPDRASSV
     LVMSNFTPVP RYGYRIGVPS DGVWIERITT DAREYGGSGL VNGAVSSEPV PAHGRPVSLS
     LTLPPLSTIF LQGPSP
//