GLGB_SYNJA
ID GLGB_SYNJA Reviewed; 770 AA.
AC Q2JT08;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=CYA_2062;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(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; CP000239; ABD00202.1; -; Genomic_DNA.
DR RefSeq; WP_011430876.1; NC_007775.1.
DR AlphaFoldDB; Q2JT08; -.
DR SMR; Q2JT08; -.
DR STRING; 321327.CYA_2062; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q2JT08; -.
DR EnsemblBacteria; ABD00202; ABD00202; CYA_2062.
DR KEGG; cya:CYA_2062; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_3; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000008818; 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; Transferase.
FT CHAIN 1..770
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260709"
FT ACT_SITE 437
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 770 AA; 89561 MW; 007E7EAF14CBEF91 CRC64;
MGFLLSAEQV LQFVTNQWQD PYAVLGPQQI EQGETSFWLV RALVPNAKQV WLVERATGQA
YPMQPLHPET LFELCFAPGT PVPDYFLRAQ RVWDPEGQHL EEWEDPYRFP LEKVNHIGEL
DRYLFNEGNH HRIYEKLGAH PISVDGVQGV HFAVWAPNAR NVSVIGDFNH WDGRQHQMKR
LGESGIWAVF IPGVGPGAVY KYEVKTAWGD IYEKSDPYGF QQEVRPKTGS IVADLHTYTW
HDQEWLEKRA ATDPLRSPIS VYEVHLGSWM HASTEDPPAD GHLVPVEQKP NTRFLTYREL
ADKLIPYVKE LGFTHIELLP VAEHPFDGSW GYQVIGYYAV TSRYGSPQDF MYFVDRAHQE
GIGVIVDWVP GHFPKDGHGL AFFDGTHLYE YADPRKGEHK GWGTLVFNYG RNEVRNYLIA
NALFWFDKYH IDGLRVDAVA SMLYLDYDRK EWIPNCYGGR EHLEAIDFFR QLNTLIFKYY
PGVLSIAEES TAWPMVTWPT HVGGLGFNLK WNMGWMHDML NYFRMDPWFR QFHHNLVTFS
LMYAFSENYM LAFSHDEVVH GKSHMLGKMP GDLWHKFASL RALYGYMFTH PGKKTLFMSM
EFGQWNEWNV WADLDWELLQ YEPHAKLRHY VATLNQLLRS QPALYTQDTK PEGFRWIDCS
DHRGIISFIR YGEDPREWLV VVCNFTPVVW PNYRIGVPQR GFYRELLNSD AVEFWGSGVG
NLGGKWTDDW PYHNLPYSLE LCLPPLSTLV LKWQPPQLAE DSGENKAMLE
