ID   GLGB_BUTFI              Reviewed;         639 AA.
AC   P30539;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 102.
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   Butyrivibrio fibrisolvens.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=H17C;
RX   PubMed=1938880; DOI=10.1128/jb.173.21.6732-6741.1991;
RA   Rumbak E., Rawlings D.E., Lindsey G.G., Woods D.R.;
RT   "Characterization of the Butyrivibrio fibrisolvens glgB gene, which encodes
RT   a glycogen-branching enzyme with starch-clearing activity.";
RL   J. Bacteriol. 173:6732-6741(1991).
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; M64980; AAA23007.1; -; Genomic_DNA.
DR   PIR; B41328; B41328.
DR   AlphaFoldDB; P30539; -.
DR   SMR; P30539; -.
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; IDA:CACAO.
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   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   TIGRFAMs; TIGR01515; branching_enzym; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycogen biosynthesis;
KW   Glycogen metabolism; Glycosyltransferase; Transferase.
FT   CHAIN           1..639
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000188690"
FT   ACT_SITE        313
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        366
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   639 AA;  73876 MW;  DC93B72A5F28C2AF CRC64;
     MSQKVFISED DEYLFGQGTH YDIYDKLGAH PSEEKGKKGF FFAVWAPNAA DVHVVGDFNG
     WDENAHQMKR SKTGNIWTLF IPGVAIGALY KFLITAQDGR KLYKADPYAN YAELRPGNAS
     RTTDLSGFKW SDSKWYESLK GKDMNRQPIA IYECHIGSWM KHPDGTEDGF YTYRQFADRI
     VEYLKEMKYT HIELIGIAEH PFDGSWGYQV TGYYAPTARY GEPTDFMYLI NQLHKHGIGV
     ILDWVPAHFC PDEFGLACFD GTCIYEDPDP RKGEHPDWGT KIFNLAKPEV KNFLIANALY
     WIRKFHIDGL RVDAVASMLY LDYGKKDGQW VPNKYGDNKN LDAIEFFKHF NSVVRGTYPN
     ILTIAEESTA WPKVTAPPEE DGLGFAFKWN MGWMHDFCEY MKLDPYFRQG AHYMMTFAMS
     YNDSENYILP LSHDEVVHLK CSMVEKMPGY KVDKYANLRV GYTYMFGHSG KKLLFMGQDF
     GQEREWSEKR ELDWFLLEND LNRGMKDYVG KLLEIYRKYP ALYEVDNDWG GFEWINADDK
     ERSTYSFYRR ASNGKDNILF VLNMTPMERK GFKVGVPFDG TYTKILDSAK ECYGGSGSSV
     PDKIKAVKGL CDYKDYSIEF DLPPYGAEVF VFQTKKTKN