GLGB_VIBVU
ID GLGB_VIBVU Reviewed; 715 AA.
AC Q8D4P0;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=VV2_1252;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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: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; AE016796; AAO08146.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8D4P0; -.
DR SMR; Q8D4P0; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAO08146; AAO08146; VV2_1252.
DR KEGG; vvu:VV2_1252; -.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002275; Chromosome 2.
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; -; 2.
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; 2.
DR TIGRFAMs; TIGR01515; branching_enzym; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..715
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188762"
FT ACT_SITE 396
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 449
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 715 AA; 81927 MW; 304C61BECF5A5F43 CRC64;
MFEKLSQAAC SEPFAFLGPF IDPTQGALRV WMPGATGVAL VLEGQPRIAL EREKESAFIL
KADLNLHLTH YQLAIDWNGV EQLVDDPYQY HGIYAEYDDL HTPKTMYQHM GSQFMTLERD
GKSISGIRFL VYAPHATAVS LVGSFNDWDG RRHPMQRLDY GIWGLFIPDL AEGVSYKFEM
KGPKGEGLPH KADPWGFYAE QYPSFASVTY DHARYQWQDA QWQTRPVTEK RKEALSFYEL
HAGSWKRNEQ GEFLNYRELA AELVPYLVDM GYTHVELMPV SEHPFYGSWG YQPVGLFAPT
SRYGSPDDFK FFVDACHQAG IGVVLDWVPA HFPSDDHGLA NFDGTPLFHD PDPRRGWHQD
WNSFIYDLGR EQVRRFLVSN ALYWFEQFHI DGIRVDAVAS MLYLDYSRSH GQWIPNMDGG
NENYDAIATL KWMNEEVYKY FPNAMTIAEE STAFPGVSAP TFMGGLGFGF KWNMGWMHDS
LSYIKEEPVH RKYHHNTLTF PLVYAHSENY VLSLSHDEVV YGKGSIHNKM PGDEWQQTAN
LRAYFGYMYG QPGKKLNFMG AEIGQTAEWN HDDQLQWFLL DFPRHQGVQA LTRDLNHLYR
NQAALHDQDC IPAGFEWRLQ DAAEQSIIAH ERISEAGERI LVVSNFTPVP RDEFRLGVPN
KGRYQLLLNT DDSKYAGSGY EVVVDAKSEA VVSEDLAQSI VLRLPPLSTL FYKLV
