GLGB_HISS2
ID GLGB_HISS2 Reviewed; 815 AA.
AC B0UU89;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=HSM_1368;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-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; CP000947; ACA31105.1; -; Genomic_DNA.
DR RefSeq; WP_012340519.1; NC_010519.1.
DR AlphaFoldDB; B0UU89; -.
DR SMR; B0UU89; -.
DR STRING; 228400.HSM_1368; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ACA31105; ACA31105; HSM_1368.
DR KEGG; hsm:HSM_1368; -.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
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..815
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000083068"
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 815 AA; 93617 MW; 744431EF7F2527B3 CRC64;
MNKFVSQSTI DTFFDGEHAD PFSVLGMHET SNGIEVRVLL PDAEKVFVLS KETKNVLCEL
LRVDERGFFA 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
IQDYVRDLNH IYQKNAPLFE LDTDPQGFEW LVVDDYQNSV FVFERRSKKD ERIIVVSNFT
PVLRQNYRFG VNIAGEYLEI LNSDAQQYMG SNSTNTSKIV TEDIESHNKA QSISIDIPPL
ATVYLKLHKV KKVRKMRKTS KVEDTAVKTE KKIAKGKTTR TKKTVADTVS EATEVKPKKT
VTKRAVVKKV KNEESAVFPN AEVIAESTSV ENNVS
