ID   GLGB_MAGSA              Reviewed;         740 AA.
AC   Q2W2Q6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 119.
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=amb3065;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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; AP007255; BAE51869.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W2Q6; -.
DR   SMR; Q2W2Q6; -.
DR   STRING; 342108.amb3065; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; mag:amb3065; -.
DR   HOGENOM; CLU_004245_3_2_5; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000007058; 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; Reference proteome; Transferase.
FT   CHAIN           1..740
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000260664"
FT   ACT_SITE        419
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        472
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   740 AA;  84012 MW;  447BD20B9AFE3040 CRC64;
     MGSSTGRRGL MPEAAKLIRS SDADAIARGR HGDPFAVLGP HAVKGGTVIR TFQPQARTVF
     VLAADGETEM SRAHPDGLFA VKLKGSPAYR LRAVRHDGGT EELDDPYRFP PVLGDLDVHL
     LAEGTHLRTF EKLGAQVRIV DGVAGVDFAL WAPNASRVSV VGDFNGWDGR RHPMRLRHEA
     GMWEIFIPGL GQGAVYKYEI VASDGRLLPL KADPYGHFAE VPPKTASVVW ELGRRDWADA
     DWMAAQKARN DRHAPISIYE VHLGSWRRVP EDCNRPLSYL EMADQLGDYV ADLGFTHVEF
     LPIHEHPFGG SWGYQPVGLF APTSRYGTPD EFRTLVDRLH QKGIGVIIDW VAGHFPNDPH
     GLHHFDGTHL YEHEDPRLGV HKDWNTLIYN YGRSEVVNYL YANALYWLEQ YHVDGLRVDA
     VASMLYLDYS REPGEWIPNR HGGNENLEAI DFLRRMNMLV YAEHPGAMTI AEESTAWPMV
     SRPVHLGGLG FGYKWNMGWM HDTLRYFSKD PIHRRYHHDS LTFAQLYAYH ENFVLPLSHD
     EVVHGKGSIF GRMPGDPWQR FANLRAYYGF MWTQPGKKLL FMGQEFAQQS EWNEDASLDW
     HLLGDGRNEG VMRLIRDLNR LYRTEPALHQ LDNEPAGFAW IDCNDRDNSV LTWLRKGFDP
     GDFLVVAGNY TPMVRDSYRI GVPEPGWYRE LLNTDSEWYG GANIHNGGGV HTEEVPWHGH
     GFSICLRLPP LATCVFKRER
//