GLGB_CUPPJ
ID GLGB_CUPPJ Reviewed; 750 AA.
AC Q46TF2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 116.
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=Reut_B4229;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000091; AAZ63582.1; -; Genomic_DNA.
DR RefSeq; WP_011300348.1; NC_007348.1.
DR AlphaFoldDB; Q46TF2; -.
DR SMR; Q46TF2; -.
DR STRING; 264198.Reut_B4229; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAZ63582; AAZ63582; Reut_B4229.
DR KEGG; reu:Reut_B4229; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_4; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
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; 1.
DR TIGRFAMs; TIGR01515; branching_enzym; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..750
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260681"
FT ACT_SITE 425
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 478
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 750 AA; 83328 MW; 7A95B1AAF97F5954 CRC64;
MNRVDTRPPE RRTQTISDGE LGALVEGRHR DPFAILGPHR DGDTLIVRAC VPGAHSVMLA
DSRGEPLAPM TPLHAGGVFT GRLPAGVSVY QLLVRWHNGT QQVSHDPYAF GLLLGELDLH
LIAEGRHFEL GACLGAQWRN VDGVQGVRFA VWAPNARRVS VIGDFNGWQP ARHPMRLRHP
SGVWELFIPE AMGARPGCRY KFDLLDPHDA QLPDKADPLA LATEAPPATA SVVTQPQVSA
PPFAWQDDEW MRLRNAVDPY AAPLSIYEVH VGSWLRAAND PARGWEVLAD RLIPYVHELG
FTHIELLPVT EHPFGGSWGY QPLSLYAPTA RLGPPQAFAA FIDRCHRDGI GVILDWVPAH
FPTDPHGLAR FDGTALYEHE DPREGFHQDW NTLIYNLGRN EVRGFLLAGA LHWLEHFHVD
GLRVDAVASM LYRDYSRAPD QWVPNRFGGR ENLEAVAFLR ELNTVVHERC PGALTIAEES
TAWPGVTASA ASGGLGFDFK WNMGWMHDTL RYLSLDPIHR AWHHQDMTFG TVYAWSEAFV
LPLSHDEVVH GKGSMLRKCP GDDWQRFAGL RAYYGFMWAH PGKKLLFMGG ELAQWQEWNH
DAELDWALLD HPMHRGVHTL VRDLNALYRE LPALHELDHS PAGFQWVVGD DHQNSVFAWL
RRPAPGSGDV VLAVTNMTPV PRYGYRIGVP SEGCWHERLN TDAACYGGSN LGNGGAVTAE
PVPSHGQEAS VLLTLPPLAT VILQHAGTQA
