ID   GLGB1_XANOM             Reviewed;         744 AA.
AC   Q2P9F7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=XOO0065;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE66820.1; -; Genomic_DNA.
DR   RefSeq; WP_011407200.1; NC_007705.1.
DR   AlphaFoldDB; Q2P9F7; -.
DR   SMR; Q2P9F7; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; xom:XOO0065; -.
DR   HOGENOM; CLU_004245_3_2_6; -.
DR   OMA; IGGFWEL; -.
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; 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; Transferase.
FT   CHAIN           1..744
FT                   /note="1,4-alpha-glucan branching enzyme GlgB 1"
FT                   /id="PRO_0000260718"
FT   ACT_SITE        422
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        475
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   744 AA;  82101 MW;  F12478404DC553B7 CRC64;
     MSERQGGQEQ DREADGVTTE GISEMSQTLQ ALADGLPVDA FAVLGPHPLA DGRRQVRVLA
     PGAEAMGLID SRGKLLARMQ ASAIDGVFEG ILSIEGPYRL RIVWPDMVQE IEDPYAFAVT
     LDESLLLQIA AGDGQALRRA LGAQHVQCGE VPGVRFAVWA PHAQRVAVVG DFNGWDVRRH
     PMRQRIGGFW ELFLPRVEAG PRYKYAVTAA DGRVLLKADP VARQTELPPA TASVVPGTDT
     FAWTDAAWMA KRDPSAVPAP LSIYEVHAAS WRRDGHNQPL DWPTLAEQLI PYVQQLRFTH
     IELLPITEHP FGGSWGYQPL GLYAPTARHG SPDGFAQFVD ACHRAGIGVI LDWVSAHFPD
     DAHGLAQFDG AALYEHADPR EGMHRDWNTL IYNYGRPEVT AYLLGSALEW IDHYHLDGLR
     VDAVASMLYR DYGRAEGEWV PNAHGGRENL EAVAFLRQLN REIAAHFPGV LTIAEESTAW
     PGVTAAISDG GLGFTHKWNM GWMHDTLSYM QRDPAERAHH HSQLTFGLVY AFDERFVLPI
     SHDEVVHGTG GLLGQMPGDD WRRFANLRAY LALMWAHPGD KLLFMGAEFG QWADWNHDQS
     LDWHLLEGAR HRGVQLLVGD LNATLRRTPA LYRGTHRAKG FDWSVADDAR NSVLAFIRHD
     PDGGGVPLLA VSNLTAQPLH DYGVGVPRAG AWREILNTDS AHYGGSNLGN SGRLATEPMG
     MHGHAQRLRL TLPPLATIYL QAEK