ID   GLGB_PROM9              Reviewed;         754 AA.
AC   Q31BV0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 121.
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};
GN   OrderedLocusNames=PMT9312_0584;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
RX   PubMed=16556843; DOI=10.1126/science.1122050;
RA   Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
RA   Delong E.F., Chisholm S.W.;
RT   "Genomic islands and the ecology and evolution of Prochlorococcus.";
RL   Science 311:1768-1770(2006).
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; CP000111; ABB49645.1; -; Genomic_DNA.
DR   RefSeq; WP_011376140.1; NC_007577.1.
DR   AlphaFoldDB; Q31BV0; -.
DR   SMR; Q31BV0; -.
DR   STRING; 74546.PMT9312_0584; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; pmi:PMT9312_0584; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_3; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000002715; Chromosome.
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; cd11322; AmyAc_Glg_BE; 1.
DR   CDD; cd02855; E_set_GBE_prok_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; 2.
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   NCBIfam; TIGR01515; branching_enzym; 1.
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; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..754
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000260674"
FT   ACT_SITE        431
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        484
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   754 AA;  88105 MW;  85AD345711FA815E CRC64;
     MIETIQADWI QSEAINLENC CNDNPLKILG PHFYEEQWVI RVWMPEADEV KINFKNNTYK
     AESINHKWLF EAILPENPES NYEINISRGG ITHTQHDPWS YIEEWMGEVD RHLFAEGNHH
     HIWEKMGAHL IEEKNQKGVM FCIWAPNAKS ISIIGDINSW DGRHHPMQKR LGGIWELFMP
     TMEEGDTYKY EIRTQQGHIY EKADPYGFLH EIRPQNGSIV SKLKNFNWND NAWITNRDSS
     SQINKPISVY EMHLGSWLHE STDNKYIEDN GNPRNPVPAA DLKPGTRLLT YPELTEKLIP
     YVKDRGFTHI ELMPISEHPF DGSWGYQVTG WYAPTSRFGT PNEFREFVNK CHEEGIGVIL
     DWVPGHFPKD KHGLAFFDGC HLYEHGDSRI GEHKEWGTLI FNYSRNEVRN FLVANLVYWF
     EEFHIDGIRV DAVASMLYRD YLRPDGEWIP NENGGNENIE AVKFLQQANH VLFQHFPGAL
     SIAEESTTWP MVTKPTDMGG LGFNLKWNMG WMHDMLDYFE IDPWFRQFHQ NSVTFSITYN
     YTENFMLALS HDEVVHGKSH LLHKMPGDDW KKYANTRALL TYMWTHPGKK TIFMGMEFGQ
     RQEWNVWDDL QWDLLEFEPH KGIRNLVDDL NALYKNEPAL WKNDFDPYGF QWIDCNDKSN
     SVISFMRREN DTNEWLVIVA NFTPNTHDSY KVGVPVEGFY KEIFNSDGSR YGGSNKGNMG
     GKEAINYNIH DYQNALELAL PPLSVSIFKH QSKK
//