ID   GLGB_CERS4              Reviewed;         728 AA.
AC   Q3J3M6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=RHOS4_10400; ORFNames=RSP_2448;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC
RC   12203 / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000143; ABA78608.1; -; Genomic_DNA.
DR   RefSeq; WP_011337498.1; NZ_CP030271.1.
DR   RefSeq; YP_352509.1; NC_007493.2.
DR   AlphaFoldDB; Q3J3M6; -.
DR   SMR; Q3J3M6; -.
DR   STRING; 272943.RSP_2448; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   DNASU; 3720044; -.
DR   EnsemblBacteria; ABA78608; ABA78608; RSP_2448.
DR   KEGG; rsp:RSP_2448; -.
DR   PATRIC; fig|272943.9.peg.1366; -.
DR   eggNOG; COG0296; Bacteria.
DR   OrthoDB; 9800174at2; -.
DR   PhylomeDB; Q3J3M6; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000002703; Chromosome 1.
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..728
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000260686"
FT   ACT_SITE        409
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        462
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   728 AA;  81458 MW;  C4B3DDDC265B7161 CRC64;
     MNVTSKPGEL VPESDVAAIM RGTHGDPFRV LGMHGGGGAP LSVRVFAPQA AEVAVLGQGG
     EVLAPLERIG AEGFFAGTVP GEEKFPYRLR FVSGPHEWEA DDPYRFPEVL GELDEYLLGE
     GRHYQLYTRL GAHPAEIEGV QGVSFAVWAP NARRVSVVGA FNAWDGRRHP MRKRIGVGVW
     ELFVPGLHTG DLYKYELLGP SGERLPLKSD PLSFAQEAPP ATASVVHGLP EAEWHDAGWM
     QERESRQRRD APISIYEVHA GSWRQGLDYD ALAEELSAYV REMGFTHVEF LPISEHPFTG
     SWGYQPIGLF APTARFGPPE GFARLVDRLH RDGIGVILDW VPAHFPSDAH GLANFDGTHL
     YDHADPRQGF HRDWNTQIYN FGRQEVANFL QASALFWLDR YHVDALRVDA VASMLYLDYS
     RNAGEWVPNR HGGRENLEAI DFLRGVNERV RLDHPGCITI AEESTAFPQV SRPVEDGGLG
     FGFKWNMGWM HDTLGYFRRD PIHRKHHQND LTFGMVYAYS EDFVLPLSHD EVVHGKGSLI
     GQMAGDRWQK FANLRAYFGF MWAHPGKKLL FMGGEFAQER EWNHDASLDW HLLDDPSHAG
     MKRLVADLNR EYRKRPALHR MDCDPEGFEW IDAGDSENSV LSFLRKAPGE KPVLAVCNLT
     PVVRSDYRIG VPEGGEWREI LNSDAAIYGG SDVGNPGGLQ AEEFSWHGRP ASLRLTLPPL
     ATIFVTPA
//