ID A0A1G7R3L0_9SPHI Unreviewed; 748 AA.
AC A0A1G7R3L0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000256|HAMAP-Rule:MF_00685};
DE EC=2.4.1.18 {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE Short=BE {ECO:0000256|HAMAP-Rule:MF_00685};
GN Name=glgB {ECO:0000256|HAMAP-Rule:MF_00685};
GN ORFNames=SAMN05192573_102116 {ECO:0000313|EMBL:SDG05353.1};
OS Mucilaginibacter gossypii.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=551996 {ECO:0000313|EMBL:SDG05353.1, ECO:0000313|Proteomes:UP000199705};
RN [1] {ECO:0000313|EMBL:SDG05353.1, ECO:0000313|Proteomes:UP000199705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gh-67 {ECO:0000313|EMBL:SDG05353.1,
RC ECO:0000313|Proteomes:UP000199705};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000826, ECO:0000256|HAMAP-
CC Rule:MF_00685};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000, ECO:0000256|HAMAP-
CC Rule:MF_00685}.
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DR EMBL; FNCG01000002; SDG05353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7R3L0; -.
DR STRING; 551996.SAMN05192573_102116; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000199705; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 258..599
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 470
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 748 AA; 85664 MW; F82F9CBC8914248A CRC64;
MAKKTTKTEN PLPDTKPVKE KKAVTKVKAD KVTPETGAPE PKKTVKTKTV AAEKPAVAEK
AVPVKTKSTA DEKPSVVKKA ASAKSKAVNA NNLTEITPQP VTLKAVEPYS RFTDFDISLF
KSGKHYKLYE KLGSHVVEYL GVIGTYFAVW APNAQYVAVI GNFNGWDRGS HSLNARWDSS
GIWEGFIPNV GNGETYKYYI KSSTGEDLEK SDPFALRWEL PPRTASIVAD TFYEWKDQDW
MQNRHEHNAL DRPYSVYEVH LGSWARNPES PDEFLTYTQL AEKMVPYVKE MGFTHVEFMP
IMEHPYYPSW GYQVSGYFAA ASRYGTPQQL MYLIEEFHKA GIGVILDWVP SHFPGDIHAL
YKFDGTHLYE HADARKGFHP DWKSYIFNYG RNEVRAFLIS NALFWLERYH ADGLRVDAVA
SMLYLDYSRK HGEWEANRYG GNENLEAISF LKEFNEAVYS HFPSVQTIAE ESTSFTGVSR
PVYLGGLGFG MKWMMGWMHD TIDYFHEDPI HRKYHHNEIT FSTIYAFTEN FMLPFSHDEV
VYGKGSMLRK MPGDEWRQFA NLRLMYGYMF THPGSKLLFM GGEFGQGDEW DFGKSLQWHV
LQYPNHQGIS ETVKALNHLY RTEPALYEKA FSHQGFEWVD GGNANDSILV YRRMGHDTKN
DLMVILNMTP VVRRDYRIGV PAAGKWKEIF NSDNEKYWGS GIINYEPVNS DQVSWHGKSQ
SIKITIPPLA AAVFKLVPDV PAKYELKR
//
