ID   GLGB_DICCH              Reviewed;         731 AA.
AC   Q8GQC5;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB;
DE            EC=2.4.1.18;
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase;
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme;
DE   AltName: Full=Glycogen branching enzyme;
DE            Short=BE;
GN   Name=glgB;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6, AND
RP   CHARACTERIZATION.
RC   STRAIN=PY35;
RX   PubMed=12480526; DOI=10.1016/s0006-291x(02)02763-8;
RA   Lim W.-J., Park S.-R., Kim M.-K., An C.-L., Yun H.-J., Hong S.-Y.,
RA   Kim E.-J., Shin E.-C., Lee S.-W., Lim Y.-P., Yun H.-D.;
RT   "Cloning and characterization of the glycogen branching enzyme gene
RT   existing in tandem with the glycogen debranching enzyme from Pectobacterium
RT   chrysanthemi PY35.";
RL   Biochem. Biophys. Res. Commun. 300:93-101(2003).
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.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.;
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.;
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF434710; AAN64024.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GQC5; -.
DR   SMR; Q8GQC5; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q8GQC5; -.
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; -; 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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycogen biosynthesis;
KW   Glycogen metabolism; Glycosyltransferase; Transferase.
FT   CHAIN           1..731
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000188705"
FT   ACT_SITE        409
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        462
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   731 AA;  83859 MW;  976E2777C7FC5F0F CRC64;
     MFVAAMTESD QNIINLLFSG HYADPFAVLG MHDTASGLEV RALLPDAIDV WVVDAHSGRK
     VANLQCRDPR GFFASAIPRR KKPFSYRLAV TWPQDTQVID DPYRFGTLLQ ELDIWLLAEG
     RHLRPFETLG AHPSTLDGVV GTCFAVWAPN AQRVSVVGDF NFWDGRRHPM RRRRENGVWE
     LFVPGVGPGQ LYKFEIIDCY GNVLVKSDPY AFESQMRPDT ASVVSRLPPA LPVDEARQHA
     NELQSPISIY EVHLGSWRRH THNNFWLSYR ELADQLVPYV KEMGFTHVEL MPVHKHPFDG
     SWGYQPLGLY APTRRFGSPD DFRYLVSAFH EAGINVLLDW VSGHFPADSY GLARFDGPAL
     YEYADPKEGY HQDWNTLIYN FDRHEVRNYL AGNALYWTER FGVDGLRVDA VASMIYRDYS
     RRDGEWVPNY FGGKENLEAI GFLRYTNQML GQHHAGAVTI AEESTDYAGV TLPPEHGGLG
     FHYKWNMGWM HDSLAYMQLD PVHRKYHHDL LTFGMLYAYS ENFVLPLSHD EVVHGKRSLL
     DRMPGDVWQK FANLRAYYGF MWAYPGKKLL FMGGEFAQGR EWNHDTSLDW HLLDEPEGWH
     AGVQQLVRDL NHCYRQHPPL YQCDYLHQGF EWVVVDDREN SVFAFIRRDA DGNEMLIISN
     FTPVPRDSYR VGINQPGAWR EVLNTDSWHY HGGNLGNQGL VYSETVGSHS RPQSLVLALP
     PLATLYLVKE A