ID   GLGB_BURTA              Reviewed;         834 AA.
AC   Q2T6R3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, 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; OrderedLocusNames=BTH_II0939;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(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: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; CP000085; ABC35639.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2T6R3; -.
DR   SMR; Q2T6R3; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q2T6R3; -.
DR   EnsemblBacteria; ABC35639; ABC35639; BTH_II0939.
DR   KEGG; bte:BTH_II0939; -.
DR   HOGENOM; CLU_004245_3_2_4; -.
DR   OMA; FGMKWMM; -.
DR   BRENDA; 2.4.1.18; 8156.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001930; Chromosome II.
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; -; 1.
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; 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..834
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000260640"
FT   ACT_SITE        511
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        565
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   834 AA;  92904 MW;  59BCF5695BFA9C18 CRC64;
     MTGIGARTAW RNAVGRRPRN ARRVSRIAYR VSRVACRVSR IAYRVSRIAY RVSRVAWRNV
     APAARRAHRP FPAVIHIASG IPLPTEPLPA PPVVVDRPAS PDDAALIAPD DLARLLRGEH
     DDPFAVLGIH AESSARDVVV RCLLPGAARV ELIDAASART LATLSPVGSG ELHAIRLPAP
     GPLRYRLRAH YADTVRDLDD PYACTPWLGS LDCHLLARGE HRDAYRRLGA HPCVHDGLEG
     TAFALWAPNA SCVSVVGSFN GWDARVHAMR KRIECGVWEL FVPGVGCGAL YKFALRTRDG
     DRLLKADPYA RRTEAPPRTA SRICAPSAFG WRDDAWMRER AAAQSAHAPI AIYEVHLDSW
     RRHPDGRAYS YDELADALIP YVAALGFTHV ELLPIAEYPF AGSWGYQPVS LFAPSARWGE
     PDALRRFVER CHLAGLGVLL DWVPAHFPQD AHGLARFDGT HLYEHEDRRV GLHRGWNTLV
     YNLGRHEVAN FLIANALYWL REFHFDGLRV DAVASMLYLD YDRDDGQWLP NVHGGRENLE
     AVAFLRRLNE TVHADAPQGA ITIAEESTAW PMVSAPVAAG GLGFDFKWNM GWMNDTLSFM
     RVDPIHRRFH LDRLTFGLLY AWSEQFVLAL SHDEVVHAKG SLLAKMPGDA WQRHANLRLY
     LAFQYAHPGK KLLFMGSEFG QEREWNHDRE LDWARLADPA SAGVRRLVGD LNRLYRRRGC
     LHRRDADSRG FRWIDCADSH QTVIAWRRIG DAPDDFVVVV CNFTPQPRTG YRIGVPAAGF
     YRELLNSDAA DYGGSGLGNL GGVSSEPVPM HGEPHSLSLL LPPLAALVFA APGH