GLGB_SYNJB
ID GLGB_SYNJB Reviewed; 763 AA.
AC Q2JK68;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=CYB_1978;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
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; CP000240; ABD02927.1; -; Genomic_DNA.
DR RefSeq; WP_011433566.1; NC_007776.1.
DR AlphaFoldDB; Q2JK68; -.
DR SMR; Q2JK68; -.
DR STRING; 321332.CYB_1978; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; cyb:CYB_1978; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_3; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001938; 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; -; 1.
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..763
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260708"
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 763 AA; 88434 MW; E71E76C8B5851489 CRC64;
MGFLLSAEQV GQFVSNQWQD PYAVLGPQQI EEAGKSFGLV RALVPNARQV WLVERATGQA
YPMQPLHPET LFELRFEPGT PLPDYFLRAQ RVWDPQGEHL EEWEDPYRFP LEKVNHIGEL
DRYLFNEGNH HRIYDKLGAH LITVDGVKGV HFAVWAPNAR NVSVIGDFNH WDGRQHQMKR
LGESGIWAVF IPGIGPGAIY KYEVKTSWGD IYEKSDPYGF QQEVRPKTGS IVADLNTYTW
HDQAWLEKRA ATDPLRSPIS VYEVHLGSWM HASAEDPPAE GQSVLVDQKP NTRFLTYREL
ADKLIPYVKE LGFTHIELLP VAEHPFDGSW GYQVIGYYAV TSRYGSPQDF MYFVDRAHQA
GIGVIVDWVP GHFPKDGHGL AFFDGTHLYE YADPRKGEHK GWGTLVFNYG RNEVRNYLVA
NALFWFEKYH IDGIRVDAVA SMLYLDYDRK EWIPNPYGGR EHLEAIDFFR QLNTLIFKYN
PGALSIAEES TAWPMVTWPT HVGGLGFNLK WNMGWMHDML DYFHMDPWFR QFHPHLVTFS
LMYAFSENYM LAFSHDEVVH GKSHMLGKMP GDHWHKFASL RALYGYMFTH PGKKTLFMSM
EFGQWNEWNV WADLDWELLQ YEPHAKLRHY VASLNHLLRS EPALYTQDTK PEGFRWIDCS
DHRGIVSFIR YGEDPSEWVV VVCNFTPVVW PNYRIGVPER GFYRELLNSD AVEFWGSGVG
NLGGKWTDDW AYHNLPYSLE LCLPQLSTLV LKWQPPQPVE SQN
