ID   GLGB_KITAU              Reviewed;         764 AA.
AC   P52980;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 113.
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;
OS   Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC
RC   12843 / NCIMB 8234 / A-377;
RX   PubMed=8068720; DOI=10.1016/0304-4165(94)90176-7;
RA   Homerova D., Kormanec J.;
RT   "Cloning of the putative glycogen branching enzyme gene, glgB, from
RT   Streptomyces aureofaciens.";
RL   Biochim. Biophys. Acta 1200:334-336(1994).
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; L11647; AAA67437.1; -; Genomic_DNA.
DR   PIR; S47569; S47569.
DR   AlphaFoldDB; P52980; -.
DR   SMR; P52980; -.
DR   STRING; 1894.ADK78_38000; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
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; 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; 2.
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; 1.
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..764
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000188746"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        440
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        493
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   764 AA;  85325 MW;  6B45482E4A268ACF CRC64;
     MSAARQPSPT VRDKAAPEPA APAAPKGARA PRARRAAPPH GVRPAPALAA EERARLLEGR
     HHDPHAVLGA RTQRGGVAFR VLRPYAKAVT VVAKGLRTEL VDEGDGLFSG LLPLTGVPDY
     RLLVTYDSDE IEVHDPYRFL PALGELDLHL IGEGRHEELW TALGSQPMEH QGVAGTRFTV
     WAPNALGVRV TGDFSYWDAV AYPMRSLGAS GVWELFLPGV AEGALYKYEI TRPDGGRTLR
     ADPMARYAEV PPANASIVTA SRYEWQDAEW MARRGALAPH QAPMSVYELH LASWRPGLSY
     RQLAEQLPAY VKELGFTHVE LMPVAEHPFG GSWGYQVTGF YAPTSRMGTP DDFRFLVDAL
     HRAGIGVIVD WVPAHFPRDD WALAEFDGRP LYEHQDPRRA AHPDWGTLEF DYGRKEVRNF
     LVANAVYWCQ EFHVDGLRAD AVASMLYLDY SRDEGDWSPN AHGGREDLDA VALLQEMNAT
     VYRRFPGVVT IAEESTAWDG VTRPTDSGGL GFGLKWNMGW MHDTLRYVSK EPVHRKYHHH
     DMTFGMVYAF SENFVLPISH DEVVHGKRSL VSKMPGDWWQ QRATHRAYLG FMWAHPGKQL
     LFMGQEFAQG SEWSETYGPD WWVLDSSYPA AGDHLGVRSL VRDLNRTYTA SPALWERDSV
     PEGFAWVEAD AADDNVFAFL RFARDGSPLL CVSNFSPVVR HGYRIGVPQE VGQWREVLNT
     DLEPYGGSGV HHARALRPEP VPAQGRAVSL RMTLPPMATV WLRP
//