GLGB_HAES1
ID GLGB_HAES1 Reviewed; 807 AA.
AC Q0I3H7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=HS_0889;
OS Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=205914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129Pt;
RX PubMed=17172329; DOI=10.1128/jb.01422-06;
RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA Xie G., Inzana T.J.;
RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT influenzae Rd.";
RL J. Bacteriol. 189:1890-1898(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; CP000436; ABI25164.1; -; Genomic_DNA.
DR RefSeq; WP_011609042.1; NC_008309.1.
DR AlphaFoldDB; Q0I3H7; -.
DR SMR; Q0I3H7; -.
DR STRING; 205914.HS_0889; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABI25164; ABI25164; HS_0889.
DR KEGG; hso:HS_0889; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
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..807
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260661"
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 807 AA; 92734 MW; 3A0332ECCEC121B7 CRC64;
MNKFVSQSTI DTFFDGKHAD PFSVLGMHET SNGIEVRVLL PDAEKVFVLS KETKNVLCEL
SRVDERGFFA GVVPNTHSFF AYQLEVYWGN EAQVIEDPYA FHPMINELDN WLLAEGSHKR
PYEILGAHFT ECDNVAGVNF RLWAPNAKRV SVVGDFNYWD GRRHPMRFHQ SSGIWELFLP
KVSLGQLYKF ELLDCHNQLR LKADPYAFSS QLRPDTASQI GALPEIVSMT EKRRKANQAD
QPISIYEVHL GSWRRNLENN FWLDYDQIAE ELIPYVKDMG FTHIELLPLS EFPFDGSWGY
QPIGLYSPTS RFGTAEGFKR LVNKAHKAGI NVILDWVPGH FPSDTHGLVA FDGTALYEHA
DPKEGYHQDW NTLIYNYGRH EVKNYLASNA LYWMERFGLD GIRVDAVASM IYRDYSREDG
QWIPNQYGGR ENLEAIEFLK QTNHLLGTEI PGVVSIAEES TSFAGVTHPP YEGGLGFHFK
WNMGWMNDTL SYMKKDPIYR QHHHSQMTFG MVYQYSENFI LPLSHDEVVH GKCSLLGKMP
GDAWQKFANL RAYYGYMWGY PGKKLLFMGN EFAQGREWNY QESLDWYLLD EFHGGGWHKA
VQDYVRDLNH IYQKNAPLFE LDTDPQGFEW LVVDDYQNSV FVFERRSKKD ERIIVISNFT
PVLRQNYRFG VNIAGEYMEI LNSDAQQYMG SNSTNTSKIV TEDIESHNKA QSISIDIPPL
ATVYLKLHKV KKVRKMRKTS KVEDTAVKTE KKIAKGKTTR TKKTVADTVS EATEVKPKKT
VTKRAVVKKV KNAEVIAEST SVENNVS
