GLGB2_CLOPE
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 25-MAY-2022, entry version 120.
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; 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; 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 EnsemblBacteria; BAB81294; BAB81294; BAB81294.
DR KEGG; cpe:CPE1588; -.
DR HOGENOM; CLU_004245_4_0_9; -.
DR OMA; IPDYWIK; -.
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..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