GLGB_LIGS1
ID GLGB_LIGS1 Reviewed; 649 AA.
AC Q1WSM8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000255|HAMAP-Rule:MF_00685};
DE EC=2.4.1.18 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE Short=BE {ECO:0000255|HAMAP-Rule:MF_00685};
GN Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=LSL_1294;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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:0000255|HAMAP-
CC Rule:MF_00685}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00685};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00685}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00685}.
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DR EMBL; CP000233; ABE00101.1; -; Genomic_DNA.
DR RefSeq; WP_011476259.1; NC_007929.1.
DR RefSeq; YP_536184.1; NC_007929.1.
DR AlphaFoldDB; Q1WSM8; -.
DR SMR; Q1WSM8; -.
DR STRING; 362948.LSL_1294; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABE00101; ABE00101; LSL_1294.
DR KEGG; lsl:LSL_1294; -.
DR PATRIC; fig|362948.14.peg.1368; -.
DR HOGENOM; CLU_004245_4_0_9; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000006559; 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..649
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260663"
FT ACT_SITE 315
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 366
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 649 AA; 76186 MW; 3C1AC6475F0C4921 CRC64;
MAVNTEERHG QESLENHKHM FNQGVNYELY NFLGVHKISR DDESGYVFRV WAPHAKQVWV
CGDFNNWDKS HPMILDEKSG IWSIEVKESR ENQYYKYLVK QANGREIMKT DPMAQVYEKR
PETAAVVKEL EPFKWNDGLW RGRQKRMNHF NNPINIYEVH APSWKEHEDG SLYTFKDLTA
ELIPYVKKMG YTHIEFMPLM EHPLPASWGY QLTGYFALCS SYGTPDEFKD FVNECHQNNI
GVLVDWVPGH FSINDDALAY YDGTPTYEYE DPDRAKNIGW GALNFDLGKP EVQSFLLSSA
FYWLNEFHLD GMRVDAVSNM IYLDYDEGPW KPNKYGDTRN LEGYAFLQKF NKVVKFAHPE
SLIIAEESSS GTQISGTIES GAIGFDYKWN MGWMNDVLEF FEMDPYFRKD NLNLVTFSFM
YWQAENFVLP LSHDEVVHGK KSLMHKMWGD RYRQFAQLRT LYTFMMMHPG KKLLFMSGEW
GQFLEWKFDH GLEWVDLQDE MNAKMQHFTS VLNHFYKEER PLWELGQQDA TLEVIDADNH
NDTVLSFIRH GKRKKDFLIV ILNFTPVERR NFRIGVPYEG TYTEILNTEM KEFGGTWVEH
NADSVSEEVN FKDYEHSITT TVPALGAIIL KPKDIKVTRR SSKKHSHKK
