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   03-AUG-2022, entry version 93.
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.ENSFCAP00000025102; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GeneID; 493962; -.
DR   KEGG; fca:493962; -.
DR   CTD; 2632; -.
DR   eggNOG; KOG0470; Eukaryota.
DR   InParanoid; Q6T308; -.
DR   OrthoDB; 165238at2759; -.
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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0005978; P:glycogen biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 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; 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.
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