ID   GLGB_DICDI              Reviewed;         678 AA.
AC   Q555Q9; Q8T189;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=1,4-alpha-glucan-branching enzyme;
DE            EC=2.4.1.18;
DE   AltName: Full=Glycogen-branching enzyme;
GN   Name=glgB; ORFNames=DDB_G0274105;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- 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; AAFI02000012; EAL69945.1; -; Genomic_DNA.
DR   RefSeq; XP_644004.1; XM_638912.1.
DR   AlphaFoldDB; Q555Q9; -.
DR   SMR; Q555Q9; -.
DR   STRING; 44689.Q555Q9; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; 44689-DDB0214943; -.
DR   EnsemblProtists; EAL69945; EAL69945; DDB_G0274105.
DR   GeneID; 8619432; -.
DR   KEGG; ddi:DDB_G0274105; -.
DR   dictyBase; DDB_G0274105; glgB.
DR   eggNOG; KOG0470; Eukaryota.
DR   HOGENOM; CLU_011131_2_2_1; -.
DR   InParanoid; Q555Q9; -.
DR   OMA; YEMHLGS; -.
DR   PhylomeDB; Q555Q9; -.
DR   UniPathway; UPA00164; -.
DR   PRO; PR:Q555Q9; -.
DR   Proteomes; UP000002195; Chromosome 2.
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   3: Inferred from homology;
KW   Glycogen biosynthesis; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..678
FT                   /note="1,4-alpha-glucan-branching enzyme"
FT                   /id="PRO_0000327602"
FT   ACT_SITE        338
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        391
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   678 AA;  78891 MW;  878594DD748805D7 CRC64;
     MTDYSKATDG TKVIHDDPWL EPYKEVIKRR HNQVKNTIQK LEESEGSLLK FSQGYEYFGF
     NVTKDGVNYR EWLPSAHEVY LVGDFNQWNK TSHPLERDNY GRWSIFIPNN SNGECAIPHG
     SKIKIYLKLA NGNFDYRIPA WIKRVEQTKE NPVFDGVFWN PSKQYVFKNK SPMKPTELRI
     YEAHVGMSSE LPEISTYSKF KDTVLPMVKE LGYNCIQLMA VMEHAYYASF GYQVTNFFAI
     SSRFGTPEEL KEMIDKAHEM GLLVFLDVVH SHASKNVLDG LNQLDGTDHH YFHSGGRGNH
     ELWDSRLFNY GNWEVMRFLL SNLRFYVDEY HFDGFRFDGV TSMIYTHHGL SPACSYDDYF
     GGAVDEDALN YLTLANVMLH TLNPSIVTIA EEVTGLATLC RPFSEGGGDF DYRLAMGIPD
     KWIELVKEKK DEDWNMGTIA HMLSNRRYKE KNIAYAESHD QSLVGDKTLA FWLMDKEMYT
     NMSVTTEETP IIDRGMSLHK MIRLITSSLG GDGYLNFMGN EFGHPEWVDF PREGNNNSLH
     HARRRWDLYR NPLLRYKQLR DFDIAMNKAE QEFRWLSSDF AYISLKHEDD KIIVFERASL
     IFIFNFHPSK SFSDYRIGSG VPGKFINVLD SDRKEFGGHV RIGKDNYHYT EDKPWHDRKY
     SLLIYIPSRT CLVLKKVD
//