ID   GLGB2_XANOM             Reviewed;         731 AA.
AC   Q2P949;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 112.
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}; OrderedLocusNames=XOO0173;
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; BAE66928.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2P949; -.
DR   SMR; Q2P949; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; xom:XOO0173; -.
DR   HOGENOM; CLU_004245_3_2_6; -.
DR   OMA; FGMKWMM; -.
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..731
FT                   /note="1,4-alpha-glucan branching enzyme GlgB 2"
FT                   /id="PRO_0000260719"
FT   ACT_SITE        410
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        463
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   731 AA;  80781 MW;  661BA6EE50D4FAAA CRC64;
     MSGVMTAVSN RWDPGVIRAL AEARHGDAFA VLGAHRTDTG RVLRTYLPGA ERVSAVLDDG
     QTIALEAGPE PGLFAGDLPA QGGYRLRIGW PGGEQDTADP YAFGPQLSDF DLHLISEGHH
     LQLADALGAN VVEVDGVRGT RFAVWAPNAS RVAVVGDFNS WDARRHPMRL RHQSGVWELF
     VPDVGPGAHY KYQLRGPHGH ELPAKADPVA RRAELAPGTA SIVADPTPYQ WSDDGWMATR
     ARRQAHDAPM SVYEMHAGSW LREEGVDLDW DGLADRLIPY VADMGFTHVE LMPVTEHPFG
     GSWGYQPLGL FAPTARFGTP DGFARFVDRC HREGIGVIVD WVPAHFPTDA HGLAHFDGTA
     LYEHADPREG FHRDWNTLIY NHGRREVSGF LIASAMEFLQ RYHVDGLRVD AVASMLYRDY
     SRNAGEWVPN IHGGRENYET IAFLRRLNAL VREHTPGAVM IAEESTAFPG VTADVAHGGL
     GFHYKWNMGW MHDTLHYAGL DPIYRRYHHG ELTFSMVYAY SERFVLPISH DEVVHGKGSL
     LGRMPGDDWQ RFANLRAYLG FMFTHPGRKL LFMGCEFGQP TEWNHDSGLP WHLLDDPRHR
     GVQTLVRDVN RLYVQYPALH AHDDDPSGFA WVVGDDAGNS VVAFLRKGKR GDAPVLVVIN
     FTPVVQHGYR IGVPQGGQWR EVFNSDAGIY GGANLGNGGI VTAEQQSMHG HAHALPLLLP
     PLGAIVLTPP G