ID   GLGB1_CLOPE             Reviewed;         674 AA.
AC   Q8XPA2;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB 1;
DE            EC=2.4.1.18;
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase 1;
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme 1;
DE   AltName: Full=Glycogen branching enzyme 1;
DE            Short=BE 1;
GN   Name=glgB1; OrderedLocusNames=CPE0063;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB79769.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8XPA2; -.
DR   SMR; Q8XPA2; -.
DR   STRING; 195102.gene:10489299; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; BAB79769; BAB79769; BAB79769.
DR   KEGG; cpe:CPE0063; -.
DR   HOGENOM; CLU_004245_4_0_9; -.
DR   OMA; FGMKWMM; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000818; Chromosome.
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; 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; Reference proteome; Transferase.
FT   CHAIN           1..674
FT                   /note="1,4-alpha-glucan branching enzyme GlgB 1"
FT                   /id="PRO_0000188695"
FT   ACT_SITE        336
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        389
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   674 AA;  80323 MW;  0178859EB7CC70DB CRC64;
     MTLVEVKDDK LEIKPVRLRK EKYKTQLKNK IFNEDDLYLF HEGRNYNAYN FMGAHFTSEN
     RKRGVRFTLW APRAKNIFLV GDFSNWETKE ENKLERINET GLWSIFIPRL KEGIKYKYYI
     EQEDGKAVLK ADPYGIYSEV RPNTASILCE KTKIRWSDKK WLNKREETNY FESPINIYEL
     HLGSWKRKDE DEFLSYDELS IILPKYIKEM GYTHVEFMPL NEHPLDASWG YQVTGYYSIT
     SRYGDIKGLK RLINALHKED IGVILDWVPG HFCKDEQGLY MFDGTPTYEY EEKWKADNKG
     WGTFNFDLGK PEVKSFLISN AFYFINEFHI DGLRVDAVSN MLYLNYGRNH GEWVPNIYGG
     NENLEAIQFI KELNEAIKTY SKGVITIAEE STSWPNVTND TEYGGLGFDF KWNMGWMNDT
     LEYNELDPIY RKYHHNKLTF PMMYNHSEKF ILPISHDEVV HGKKSLIDKM QGDYWNKLAN
     LRAYMAYMYG HPGKKLMFMG CEFGQFIEWR EYEELEWKLI DKFDMHRKTH NFFKDLNNFY
     KNNSELWELD YDQDGFQWID ADNNEQSIYI FIRKSKNIEK YKIFVCNFTP MVYYDFNIGV
     PEKGVYREIF NTDKEEYGGS GQVIKGNLFS RKGWCHNQQY TLTIKVPPMA VSVFERIIEE
     NKTEEKIVKE DKYI