GLGB2_STRCO
ID GLGB2_STRCO Reviewed; 741 AA.
AC Q59832; Q9KY06;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB 2;
DE EC=2.4.1.18;
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase 2;
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme 2;
DE AltName: Full=Glycogen branching enzyme 2;
DE Short=BE 2;
GN Name=glgB2; Synonyms=glgBII; OrderedLocusNames=SCO7332;
GN ORFNames=SC4G10.11c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=8596463; DOI=10.1111/j.1365-2958.1995.mmi_18010089.x;
RA Bruton C.J., Plaskitt K.A., Chater K.F.;
RT "Tissue-specific glycogen branching isoenzymes in a multicellular
RT prokaryote, Streptomyces coelicolor A3(2).";
RL Mol. Microbiol. 18:89-99(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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:0000250}.
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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; X73903; CAA52109.1; -; Genomic_DNA.
DR EMBL; AL939131; CAB92878.1; -; Genomic_DNA.
DR PIR; S70078; S34218.
DR RefSeq; NP_631386.1; NC_003888.3.
DR RefSeq; WP_011031592.1; NZ_VNID01000019.1.
DR AlphaFoldDB; Q59832; -.
DR SMR; Q59832; -.
DR STRING; 100226.SCO7332; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 1102770; -.
DR KEGG; sco:SCO7332; -.
DR PATRIC; fig|100226.15.peg.7436; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_11; -.
DR InParanoid; Q59832; -.
DR OMA; DKRRQPI; -.
DR PhylomeDB; Q59832; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001973; 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; 1.
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..741
FT /note="1,4-alpha-glucan branching enzyme GlgB 2"
FT /id="PRO_0000188750"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 421
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 474
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CONFLICT 561
FT /note="Q -> H (in Ref. 1; CAA52109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 82776 MW; 5FB7A44120677759 CRC64;
MALRDTSIPE PSGPVPPAPG ACATAPPLDP TDRGRLLAGA HHDPHSLLGA HPVPGGIAFR
VLRPFAREVG VVVDGERHTL ASEEDGLFSG VLPLAGIPSY TLVVAYEQGE TQETHDPYRF
LPALGELDLH LIGEGRHEQL WQALGAEPMT HEGVTGTRFT VWAPNAQGVR VATDFTHWDG
TAFPMRSLGS SGVWELFLPG VGEGTRYKFE IHSRYGHRFL KADPMARAAE EPPNTASVVT
ASRYEWGDAQ WMRTRADTPV HEAPFSVYEV HLPSWRPGLT YRELAEELPA YVKDLGFTHV
ELMPVAEHPY GPSWGYQVTG FYAPTARLGS PDDFRFLVDA LHRAGIGVIM DWVPAHFPKD
DWALGRFDGD PLYEPGDSRR AEHPDWGTYT FDFARTEVRN FLVANAVYWC EEFHIDGLRV
DAVASMLYLD YSRDSGQWEP NQYGGREDLA AMAFLQEMNA TVYRRCPGVV TIAEESTAWG
GVTRPTDTGG LGFGLKWNMG WMHDSLEYVA HEPVHRRYHH HEMTFSMVYA YSENYVLPIS
HDEVVHGKQA LVSKMPGDWW QRRANVRAYL GFMWAHPGKQ LLFMGQEFAQ GAEWSEKQGP
EWWLLDEGYH SAGDHRGVQD LVRELNTRYT RTPALWQRDT DPAGFRWVSV DAAEDNVFAF
LRYGTDGTPL LAVSNFSPVV RHEYGLAVGD EAVAWQEVLN TDAEEYGGGG VGNPDPVKPE
DGSIRITLPP LATVWLMPYA L
