GLGB_RHOBA
ID GLGB_RHOBA Reviewed; 736 AA.
AC Q7UVH1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 114.
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=RB2638;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294137; CAD72753.1; -; Genomic_DNA.
DR RefSeq; NP_865069.1; NC_005027.1.
DR RefSeq; WP_007324338.1; NC_005027.1.
DR AlphaFoldDB; Q7UVH1; -.
DR SMR; Q7UVH1; -.
DR STRING; 243090.RB2638; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; CAD72753; CAD72753; RB2638.
DR KEGG; rba:RB2638; -.
DR PATRIC; fig|243090.15.peg.1210; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_0; -.
DR InParanoid; Q7UVH1; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..736
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188736"
FT ACT_SITE 415
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 468
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 736 AA; 83639 MW; ADD83793F4B9327D CRC64;
MNSQLSLSTI QSLVDGSVAN PGSLLGRHPV NYRGREATSV RVLEPNAESV WLIDSASGLR
RPMRRLHPGG FFEAICDEPI TKPSTSRLQM IDKTGKEIKT TSPYTVPSIF SDLDRYLIGE
GRHNQLYERL GAQLREVDGV KGVNFAVWAP NARSVQVVGD FNGWDGRGHV AQPVESTGIW
ELFLPGATVG QKYKFRIQTQ HGHWMDKCDP MAFAAELPPL TANIITDINT YSWNDSDWLQ
QRAEMDPMHT PMNVYEVHLG SWQKGPGRTH GWLDYRDLAK RLVDYCHRMN FTHVELMPIS
EHPFTGSWGY QSVGYYAPTS RHGSPEDFMF FVDHMHQNGI GVLIDWVPAH FPKDDHGLRQ
FDGSALYEHA DPRQGEHPDW GTMIFNFGRN EVKNFLIANA LFWLDKYHID GLRVDAVASM
LYLDYSREDG EWIPNRYGGR ENLESIDFLR DFNIAVHENH PGVITAAEES TAWPGVSRPT
YDGGLGFTYK WNMGWMNDTL SYMRNEPIHR KFHQNELTFS LIYAFTENFT LPLSHDEVVH
GKGSLISQMP GDMWQKFANL RLLYSYMWTH PGKKLLFMGG EIAQWTEWNA DDGPQWELLD
FDTHRGVQQL VADLNKVVIE NPALHWHDFT GDGFEWIDAH NAEDSVLVYL RKGAEGDPPI
LVCNNFTPVP RDNYRVGVPA QGFWKEIFNS DGEAYGGSNL GNYPGCQTTG IEHHARPDSI
EVTLPPLGTT ILRLES
