GLGB_SHEB2
ID GLGB_SHEB2 Reviewed; 743 AA.
AC B8EAX1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 81.
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};
GN OrderedLocusNames=Sbal223_3028;
OS Shewanella baltica (strain OS223).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=407976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS223;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA Tiedje J.;
RT "Complete sequence of chromosome of Shewanella baltica OS223.";
RL Submitted (DEC-2008) 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: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; CP001252; ACK47513.1; -; Genomic_DNA.
DR RefSeq; WP_012588209.1; NC_011663.1.
DR AlphaFoldDB; B8EAX1; -.
DR SMR; B8EAX1; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ACK47513; ACK47513; Sbal223_3028.
DR KEGG; sbp:Sbal223_3028; -.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002507; 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; 1.
DR TIGRFAMs; TIGR01515; branching_enzym; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..743
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000147761"
FT ACT_SITE 416
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 469
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 743 AA; 84350 MW; 75E4854CBE07E769 CRC64;
MMTQANAYFY DGADVALLNG QYTDVFSLLG MHSANEGKAL IVRCFLRNAL SVDVISIKDG
RKVASLDKVN EQGLFAGTLG RRVKPFLYLL RVEYPQCQLD IVDPYQFDSL LNSDDIYLFG
EGSAERAYEF LGANWRQTQG VEGVHFCVWA PNAKRVSVVG DFNHWDDTRH VMRQHLANGL
WELFLPNVVE GAHYKFDLVY QNGERHAKSD PMATQMECAP HNASIVPPKA HHSWNDTAWM
SKRAATAWHK APMSAYEVHL GSWRRKGEQG EQYLDYQDLI EQLIPYVKEQ GFTHIELMPI
SEFPFDGSWG YQPVGLYAPT HRFGDANGLK AFVDACHQAG IGIILDWVSA HFPKDPHGLV
RFDGTCLYEH EDPRKGTHPD WDTLIYNYDR GEVRSFLLSN ACYWLREFHF DGLRLDAVSS
MLYLDYSREP GQWLPNTYGG RENLEAINFL QILNQRLYQA FPGICMIAEE STAFAGVTKP
TDQQGLGFGF KWNMGWMNDS LSYLGRDPLY RQFHHHQLTF SLMYAYTEQF MLSVSHDEVV
HGKGSLLHKI PGDDWQKFAT LRAYYGFMWG HPGKKLLFMG CEFGQRNEWN HNQSLDWHLL
AYEPHQGVQR WLKDLNHLYQ AMPALSVQDY EGAGFSWLDC ENSRDSIFTF VRYGLAGDAP
LVFVINMTPQ LHTGFRIGLP LAGDYREYLN SDSQIYGGSN QGNAGTVVAE SLPWQGMAQS
ALITVPPLGC LVIGPATGLA EAN
