ID GLGB_FELCA Reviewed; 699 AA.
AC Q6T308;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=1,4-alpha-glucan-branching enzyme;
DE EC=2.4.1.18 {ECO:0000250|UniProtKB:Q04446};
DE AltName: Full=Brancher enzyme;
DE AltName: Full=Glycogen-branching enzyme;
GN Name=GBE1;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISEASE.
RA Fyfe J.C., Hawkins M.G., Henthorn P.S.;
RT "Molecular characterization of feline glycogen storage disease type IV.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for normal glycogen accumulation. The alpha 1-6
CC branches of glycogen play an important role in increasing the
CC solubility of the molecule. {ECO:0000250|UniProtKB:Q04446}.
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:0000250|UniProtKB:Q04446};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000250|UniProtKB:Q04446}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q04446}.
CC -!- DOMAIN: Binds its carbohydrate substrate close to the active site, but
CC also via regions close to the N-terminus; this may result in increased
CC affinity and therefore increased catalytic efficiency.
CC {ECO:0000250|UniProtKB:Q04446}.
CC -!- DISEASE: Note=Defects in GBE1 are the cause of glycogen storage disease
CC IV (GSD-IV). {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; AY439007; AAR13899.1; -; mRNA.
DR RefSeq; NP_001009872.1; NM_001009872.1.
DR AlphaFoldDB; Q6T308; -.
DR SMR; Q6T308; -.
DR STRING; 9685.ENSFCAP00000049901; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; 9685-ENSFCAP00000025102; -.
DR GeneID; 493962; -.
DR KEGG; fca:493962; -.
DR eggNOG; KOG0470; Eukaryota.
DR InParanoid; Q6T308; -.
DR OrthoDB; 96at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR CDD; cd11321; AmyAc_bac_euk_BE; 1.
DR CDD; cd02854; E_set_GBE_euk_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
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; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 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; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 2: Evidence at transcript level;
KW Glycogen biosynthesis; Glycogen storage disease; Glycosyltransferase;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..699
FT /note="1,4-alpha-glucan-branching enzyme"
FT /id="PRO_0000188773"
FT ACT_SITE 354
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 409
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 59..60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
FT BINDING 115..118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
FT BINDING 330..333
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
FT MOD_RES 170
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q04446"
SQ SEQUENCE 699 AA; 80564 MW; 2B463AA38C5CCEA3 CRC64;
MAAPVARGEC SEAALAAALA DVPELARLLE LDPYLKPFAL DFQRRYKKFN ETLNNIGENE
GGIDKFSRGY ESFGVHRCAD GGLYCKEWAP GAEGVFLTGD FNDWNPFSYP YKKLDYGKWE
LYIPPKQNKS QLVPHGSKLK VVIRSKSGEI LYRISPWAKY VTREGENVNY DWTHWDPEHP
YKFKHSRPKK PRGVRIYESH VGISSYEGKI ASYKHFTYNV LPRIKDLGYN CIQMMAIMEH
AYYASFGYQI TSFFAASSRY GTPEELKELV DTAHSMGITV LLDVVHSHAS KNSEDGLNMF
DGTDSCYFHS GPRGNHDLWD SRLFIYSSWE VLRFLLSNIR WWLEEYGFDG FRFDGVTSML
YHHHGMGQAF SGDYHEYFGL QVDEDALIYL MLANHLVHTL YPNSITIAED VSGMPALCSP
ISQGGVGFDY RLAMAIPDKW IQLLKEFKDE DWNMGNIVYT LTNRRYLEKC IAYAESHDQA
LVGDKTLAFW LMDAEMYTNM SVLTPFTPVI DRGIQLHKMI RLITHALGGE GYLNFMGNEF
GHPEWLDFPR KGNNESYHYA RRQFHLTDDD LLRYKFLNNF DRDMNKLEER CGWLSAPQAF
VSEKHEGNKI IAFERAGLVF IFNFHPSKSY TDYRVGTTLP GKFRIVLDTD AAEYGGHQRL
DHSTEFFSQP FKHNERPCSL LVYIPNRVGL ILQNVDMPN
//
