GLGB_HAEIG
ID GLGB_HAEIG Reviewed; 730 AA.
AC A5UEJ2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=CGSHiGG_00440;
OS Haemophilus influenzae (strain PittGG).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374931;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittGG;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(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; CP000672; ABQ99197.1; -; Genomic_DNA.
DR RefSeq; WP_011962031.1; NC_009567.1.
DR AlphaFoldDB; A5UEJ2; -.
DR SMR; A5UEJ2; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; A5UEJ2; -.
DR EnsemblBacteria; ABQ99197; ABQ99197; CGSHiGG_00440.
DR KEGG; hiq:CGSHiGG_00440; -.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001990; 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; Transferase.
FT CHAIN 1..730
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000044980"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 458
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 730 AA; 83844 MW; 98AC5D5D0F8E1A51 CRC64;
MTTAVTQAII DGFFDASNGD PFATLGMHET EQGIEIRTLL PDANRMVVIE RESGKEITEL
DCVDERGFFV GVIPNCRQFF AYQLQVFWGN EAQIIEDPYR FHPMIDDLEQ WLLSEGSMLR
PYEVLGAHFM ECDGVSGVNF RLWAPNARRV SIVGDFNYWD GRRHPMRFHS KSGVWELFLP
KASLGQLYKF ELIDCHGNLR LKADPFAFSS QLRPDTASQV SALPNVVEMT EARKKANQGN
QPISIYEVHL GSWRRNLENN FWLDYDQIAD ELIPYVKEMG FTHIEFLPLS EFPFDGSWGY
QPLGLYSPTS RFGSPEAFSR LVKRAHEAGI NVILDWVPGH FPSDTHGLVA FDGTALYEHE
DPREGYHQDW NTLIYNYGRN EVKNFLSSNA LYWLERFGVD GIRVDAVASM IYRDYSRVEG
EWIPNQYGGR ENLEAIEFLK HTNWKIHSEM AGAISIAEES TSFAGVTHPS ENGGLGFNFK
WNMGWMNDTL AYMKLDPIYR QYHHNKMTFG MVYQYSENFV LPLSHDEVVH GKYSLLGKMP
GDTWQKFANL RAYYGYMWGY PGKKLLFMGN EFAQGREWNH EESLDWFLLD ENIDGGWHKG
VLKLVKDLNQ IYQKNRPLFE LDNSPEGFDW LVVDDAANSV FAFERRSSNG ERIIVVSNFT
PVPRHDYRIG VNIVGEYEEI LNTDSMYYQG SNVGNFGCVA SENIESHGRE NSISVSIPPL
ATVYLRLKAK
