ID   GLGB_BURPS              Reviewed;         738 AA.
AC   Q63T91;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB {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 {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE            Short=BE {ECO:0000255|HAMAP-Rule:MF_00685};
GN   Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685};
GN   OrderedLocusNames=BPSL2076;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH36077.1; -; Genomic_DNA.
DR   RefSeq; WP_004538410.1; NZ_CP009538.1.
DR   RefSeq; YP_108675.1; NC_006350.1.
DR   AlphaFoldDB; Q63T91; -.
DR   SMR; Q63T91; -.
DR   STRING; 272560.BPSL2076; -.
DR   KEGG; bps:BPSL2076; -.
DR   PATRIC; fig|272560.51.peg.75; -.
DR   eggNOG; COG0296; Bacteria.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000605; Chromosome 1.
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; 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; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..738
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000188689"
FT   ACT_SITE        417
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        472
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   738 AA;  81016 MW;  B1AFA639ECEF4C1D CRC64;
     MTDAPFDRAD IDALLGARHP DPFACLGPHR VGDATVVRTL LPGALRVRAI AAGGGVLGEL
     RQVDPAGCFA GALPDGQERG ERPRYRLSID WPDARQDVED AYAFGTLLDE DALARFAAGD
     PRAALACLGA RALDMDGVPG VRFAVWAPGA SRVSVVGDFN GWDARRHPMR LRRPWGVWEL
     FVPRIGAGER YKFALRARDG AALPLKADPC ACRTEAPPRT ASIVADLDAL ERFGWHDDAW
     LRARASLDLA HAPVSIYEVH PESWLRVAAE GNRSATWDEL AQRLIPYAAG MGFSHVELTP
     IAEYPFGGSW GYQSLSPFAP SARFGPPEGF ARFVEHAHAA GLGVIVDWVP AHFPDDPHGL
     GKFDGTALFE HADPREGWHP DWHTHVFNVG RREVGAFLIA SALAWAHRYH VDGIRVDAVA
     SMLYRDYSRA AGEWVPNVYG GRENLESIAF LKHFNDTLHG PAAPPGVATF AEESTAWPGV
     TAPTAEHGLG FDFKWNMGWM HDTLAYLRED PIHRRHHHDR LTFGLVYAFS ERFVLPLSHD
     EVVHGKGSLA AKMPGDAWQR LANLRAYFGF MWAHPGKKLL FMGGEFAQWG EFAHDATPQW
     DLLDAPAHRG VQRLVRDLNR LHAAEPALHA LDDRPAGFAW LVGDDRNNSV FAFVRRDDAG
     RMLVAVCNFT PVPRTDYRLG LPAPGRWAEV LNTDGAAYGG TDAGNGGAVQ ADEIPAHGER
     WSAALRLPPL ATLWLRPA
//