GLGB_FRACC
ID GLGB_FRACC Reviewed; 812 AA.
AC Q2J6Q9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
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};
GN OrderedLocusNames=Francci3_3681;
OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=106370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45818 / CECT 9043 / CcI3;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CP000249; ABD13033.1; -; Genomic_DNA.
DR RefSeq; WP_011438057.1; NZ_LRTJ01000049.1.
DR AlphaFoldDB; Q2J6Q9; -.
DR SMR; Q2J6Q9; -.
DR STRING; 106370.Francci3_3681; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABD13033; ABD13033; Francci3_3681.
DR KEGG; fra:Francci3_3681; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_11; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR PhylomeDB; Q2J6Q9; -.
DR BRENDA; 2.4.1.18; 15235.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001937; 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; -; 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..812
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260658"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 490
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 543
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 812 AA; 89229 MW; 7DA0746ADF835D01 CRC64;
MNNGDVNNGT ARTGRLATGL APDRPNPRGA ATAVRNGGGR VALADRDASS ASAQPGQTAD
DPAVPSAPPS APPSALPADP PAVAPAVSVD LPYDDLERLV SGAHHDPHAL LGAHPHPGSD
ATVVRVLRPD ARAVTVLVGP ARYPATRLHS GGVFGVAVPG MLPDYRIEVT YPDGPYLIDD
PYRHLPTLGE MDLHLIIEGR HEQLWKVLGA HPRALTTPGG ATVTGVSFAV WAPSARGVRL
VGDFDFWDGR AFPMRSLGRS GIWELFVPGA GTGARYKYEI LGFDGIWRQK ADPLAFHTEV
PPATASVVFA SDFTWNDGAW LDRRARTAWR TEPVSVYEVH LGSWRRGLSY RELAEELTAY
VVENGFTHVE MLPVAEHPFG GSWGYQVSAY YAPTARFGSP DEFRHLVDTL HRAGIGVIVD
WVPAHFPRDT WALGRFDGTP LYEHPDPRRG EQPDWGTYVF DLGRPEVRNF LVANALYWFE
EFHIDGLRVD AVASMLYLDY SRPEGGWLPN IHGGRENLDA VSFLQETNAT VYRRFPGAMM
IAEESTAWPG VTRPTHLGGL GFGFKWNMGW MHDTLDYNSR LPIHRMYHHH QMTFSMVYAY
SENFILPFSH DEVVHGKGSL LRKMPGDRWA QLANLRALLA YMWAHPGKKL LFMGCEFAQD
NEWNESASLE WPLLDDPAHA GVADLVRDLN GLYRTVPALY QHDADPAGFS WIDANDAENN
VFSFLRWSGE DPAGGVLACV TNFAGIGHEG YRIGLPFPGR WREILNTDGY RYGGGNIGNL
GSVQAVEEPH HGLDASATLT LPPLGAIWLS PA
