GLGB_SYNE7
ID GLGB_SYNE7 Reviewed; 774 AA.
AC P16954; Q31PA4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB;
DE EC=2.4.1.18;
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase;
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme;
DE AltName: Full=Glycogen branching enzyme;
DE Short=BE;
GN Name=glgB; OrderedLocusNames=Synpcc7942_1085;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2142668; DOI=10.1016/0378-1119(90)90208-9;
RA Kiel J.A.K.W., Boels J.M., Beldman G., Venema G.;
RT "Nucleotide sequence of the Synechococcus sp. PCC7942 branching enzyme gene
RT (glgB): expression in Bacillus subtilis.";
RL Gene 89:77-84(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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: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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is about 35 degrees Celsius.;
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; M31544; AAB39038.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57115.1; -; Genomic_DNA.
DR PIR; JQ0550; JQ0550.
DR RefSeq; WP_011242776.1; NC_007604.1.
DR AlphaFoldDB; P16954; -.
DR SMR; P16954; -.
DR STRING; 1140.Synpcc7942_1085; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P16954; -.
DR EnsemblBacteria; ABB57115; ABB57115; Synpcc7942_1085.
DR KEGG; syf:Synpcc7942_1085; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_3; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1085-MON; -.
DR BRENDA; 2.4.1.18; 7781.
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; 2.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..774
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188756"
FT ACT_SITE 440
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 493
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 774 AA; 89195 MW; C4C8885EF103CCE4 CRC64;
MTGTTPLPSS SLSVEQVNRI ASNQEQNPFD ILGPHPYEHE GQAGWVIRAY LPEAQEAAVI
CPALRREFAM HPVHHPHFFE TWVPEETLEI YQLRITEGER ERIIYDPYAF RSPLLTDYDI
HLFAEGNHHR IYEKLGAHPC ELENVAGVNF AVWAPSARNV SILGDFNSWD GRKHQMARRS
NGIWELFIPE LTVGAAYKYE IKNYDGHIYE KSDPYGFQQE VRPKTASIVA DLDRYTWGDA
DWLERRRHQE PLRQPISVYE VHLGSWMHAS SDAIATDAQG KPLPPVPVAD LKPGARFLTY
RELADRLIPY VLDLGYSHIE LLPIAEHPFD GSWGYQVTGY YAATSRYGSP EDFMYFVDRC
HQNGIGVILD WVPGHFPKDG HGLAFFDGTH LYEHADSRQG EHREWGTLVF NYGRHEVRNF
LAANALFWFD KYHIDGIRVD AVASMLYLDY NRKEGEWIPN EYGGRENIEA ADFLRQVNHL
IFSYFPGALS IAEESTSWPM VSWPTYVGGL GFNLKWNMGW MHDMLDYFSM DPWFRQFHQN
NVTFSIWYAF SENFMLALSH DEVVHGKSNL IGKMPGDEWQ KFANLRCLLG YMFTHPGKKT
LFMGMEFGQW AEWNVWGDLE WHLLQYEPHQ GLKQFVKDLN HLYRNAPALY SEDCNQAGFE
WIDCSDNRHS IVSFIRRAHE SDRFLVVVCN FTPQPHAHYR IGVPVAGFYR EIFNSDARSY
GGSNMGNLGG KWTDEWSCHN RPYSLDLCLP PLTTLVLELA SGPESLSEAA NSPL
