ID   GLGB1_RHIJ3             Reviewed;         735 AA.
AC   Q1MBS9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme 1 {ECO:0000255|HAMAP-Rule:MF_00685};
DE   AltName: Full=Glycogen branching enzyme 1 {ECO:0000255|HAMAP-Rule:MF_00685};
DE            Short=BE 1 {ECO:0000255|HAMAP-Rule:MF_00685};
GN   Name=glgB1 {ECO:0000255|HAMAP-Rule:MF_00685};
GN   OrderedLocusNames=RL4115;
OS   Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium
OS   leguminosarum bv. viciae).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium;
OC   Rhizobium johnstonii.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 114642 / LMG 32736 / 3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(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; AM236080; CAK09604.1; -; Genomic_DNA.
DR   RefSeq; WP_011653523.1; NC_008380.1.
DR   AlphaFoldDB; Q1MBS9; -.
DR   SMR; Q1MBS9; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; CAK09604; CAK09604; RL4115.
DR   KEGG; rle:RL4115; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_004245_3_2_5; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000006575; 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; 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   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; 1.
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..735
FT                   /note="1,4-alpha-glucan branching enzyme GlgB 1"
FT                   /id="PRO_0000260684"
FT   ACT_SITE        418
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        471
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   735 AA;  83250 MW;  C5146A79B7FCD295 CRC64;
     MKTPKTVPEV KLSWEISADE ITAILAGSHS NPFAVLGVHQ AGDAFVARCF IPGAEEVTAM
     TLDGGVIGEL KQLHADGVFA GPVSLTKLQP VRYRARRGDA EWAVTDPYSF GPVLGPMDDY
     FAREGSHLRL FDKMGAHLIK HDGAQGIHFA VWAPNAQRVS VVGDFNNWDG RRHVMRFRSD
     SGIWEIFAPD VPIGVAYKFE IRGQDGVLLP LKADPFARRS ELRPKTASVT AAELEQEWED
     EAHLKHWRET DKRRQPISIY EVHAASWQRR QDGTMLSWDE LASSLIPYCA DMGFTHIEFL
     PITEYPYDPS WGYQTTGLYA PTARFGEPEG FARFVNGCHK VGIGVILDWV PAHFPTDEHG
     LGWFDGTALY EHEDPRKGFH PDWSTAIYNF GRTEVVSYLV NNALYWAEKF HLDGLRVDAV
     ASMLYLDYSR KHGEWIPNEY GGNENLEAVR FLQDLNIRIY GKNSNVMTIA EESTSWPKVS
     QPVHEGGLGF GFKWNMGFMH DTLSYMSRDP IYRGHHHNEL TFGLLYAYSE NFVLPLSHDE
     VVHGKGSLIA KMPGDDWQKF ANLRAYYAYM WGYPGKKLLF MGQEFAQWSE WSEEKALDWN
     LLQYRMHEGM RRLVRDLNFT YRSKPALHAR DCEGEGFEWL VADDHQNSVF AWLRKAPGQK
     PVAVITNFTP IYRENYSIRL PSAGRWREIL NTDADIYGGS GKGNGGRVQA VDAGGNITCS
     ITLPPLATIM LEPEN
//