ID   GLGB2_CLOPE             Reviewed;         664 AA.
AC   Q8XK15;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB 2;
DE            EC=2.4.1.18;
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase 2;
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme 2;
DE   AltName: Full=Glycogen branching enzyme 2;
DE            Short=BE 2;
GN   Name=glgB2; OrderedLocusNames=CPE1588;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillota; 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; BAB81294.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8XK15; -.
DR   SMR; Q8XK15; -.
DR   STRING; 195102.gene:10490852; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; cpe:CPE1588; -.
DR   HOGENOM; CLU_004245_4_0_9; -.
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; 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; 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; Reference proteome; Transferase.
FT   CHAIN           1..664
FT                   /note="1,4-alpha-glucan branching enzyme GlgB 2"
FT                   /id="PRO_0000188696"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        342
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        395
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   664 AA;  77485 MW;  DFFC9DBA4024081A CRC64;
     MGGKEMRNCK ELKHEKNGNV TEKVGKNKGK SKKVSKDESL LSFDLFLEGK EHSAYKFMGA
     HFITENRKRG VRFTTWAPRA SKIYVIGDFN NWELKEEYSM KKINERGIWS LFLPKLEEGI
     KYKFAVVNEC GNNTVYKADP YAFKSELRPN TASVLTKIKS FRWGDKRWLN KREKEGLDNK
     PMNIYELHLG SWKRKDGEFM TYEEISEVLV EYIKEMGYTH VEFMPINEHP LDASWGYQGV
     GYYSVTSRYG DLNGLKTLIN KLHKNNIGVL LDWVPSHFCK DEHGLFMFDG SPTYEYEAWW
     KANNEGWGTC NFDLGRPEVK SFLFSNAMYW INEFHVDGLR VDAVSNMLYL DYGREYGEWE
     PNIYGGNGNL EAIAFLKELN TIIKKEGKGA ITVAEESTSW EGITKPVEED GLGFDYKWNM
     GWMNDTLSYI ELDPIYRKYH HNKMNFSMMY NYSEKFILPI SHDEVVHGKK SLINKMWGDD
     WKKYAGLRVY ASFMMGHPGK KLMFMGCEFG QFVEWREWEE LQWNVIEEFD IHRKTKEYFK
     ALNKFYLENS SLWSLDYEEE GFKWIDADNS EESVLSFIRI GKNKKEKLIF ICNFTPEVYY
     DFKVGVPELG EYVEAFNSDA LEFGGAGNIV GDSILKATEE SFKDFDYSIS VKVPPLGTLV
     LKVK
//