GLGB_SYNP6
ID GLGB_SYNP6 Reviewed; 774 AA.
AC Q5N4W5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=syc0464_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(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; AP008231; BAD78654.1; -; Genomic_DNA.
DR RefSeq; WP_011242776.1; NC_006576.1.
DR AlphaFoldDB; Q5N4W5; -.
DR SMR; Q5N4W5; -.
DR STRING; 269084.syc0464_c; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q5N4W5; -.
DR EnsemblBacteria; BAD78654; BAD78654; syc0464_c.
DR KEGG; syc:syc0464_c; -.
DR eggNOG; COG0296; Bacteria.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001175; 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; 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 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..774
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188755"
FT ACT_SITE 440
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 493
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
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
