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Database: UniProt
Entry: A0A0U5GI22_9GAMM
LinkDB: A0A0U5GI22_9GAMM
Original site: A0A0U5GI22_9GAMM 
ID   A0A0U5GI22_9GAMM        Unreviewed;       729 AA.
AC   A0A0U5GI22;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000256|HAMAP-Rule:MF_00685};
DE            EC=2.4.1.18 {ECO:0000256|HAMAP-Rule:MF_00685};
DE   AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000256|HAMAP-Rule:MF_00685};
DE   AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE   AltName: Full=Glycogen branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE            Short=BE {ECO:0000256|HAMAP-Rule:MF_00685};
GN   Name=glgB {ECO:0000256|HAMAP-Rule:MF_00685,
GN   ECO:0000313|EMBL:CUU22530.1};
GN   ORFNames=EM595_0293 {ECO:0000313|EMBL:CUU22530.1};
OS   Duffyella gerundensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Duffyella.
OX   NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU22530.1, ECO:0000313|Proteomes:UP000059419};
RN   [1] {ECO:0000313|Proteomes:UP000059419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Blom J.;
RL   Submitted (NOV-2015) 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.
CC       {ECO:0000256|ARBA:ARBA00002953, ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00000826, ECO:0000256|HAMAP-
CC         Rule:MF_00685};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00685}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000256|ARBA:ARBA00009000, ECO:0000256|HAMAP-
CC       Rule:MF_00685}.
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DR   EMBL; LN907827; CUU22530.1; -; Genomic_DNA.
DR   RefSeq; WP_067427185.1; NZ_LN907827.1.
DR   AlphaFoldDB; A0A0U5GI22; -.
DR   STRING; 1619313.EM595_0293; -.
DR   GeneID; 84614717; -.
DR   KEGG; ege:EM595_0293; -.
DR   PATRIC; fig|1619313.3.peg.306; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000059419; 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 {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00685};
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW   Rule:MF_00685};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP-
KW   Rule:MF_00685};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00685}; Reference proteome {ECO:0000313|Proteomes:UP000059419};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          247..596
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        405
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        458
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   729 AA;  84278 MW;  E5A5B7157775F836 CRC64;
     MSELVDRQTI NALISGHYAD PFALLGMHQT EAGLEVRALL PDASEVWVIE TKTGRKCAQL
     TCIDPRGFFS AVVPRRKNPF RYQLAVTWHD QQNLIDDAYR FGPLLQDMET WLLAEGTHLR
     PYETMGAHSA VIDGVTGTRF ILWAPNAQRV SVVGEFNFWD GRRHPMRFRR ENGMWELFVP
     GAMNGQLYKY EIIDAHGQLR LKADPYAFEA QMRPQTASMI CGLPEKVEMA EARKQANGFD
     KPISIYEVHL GSWRRHTDDN FWLSYKELEE QLIPYAVEMG FTHLELLPIS EHPFDGSWGY
     QPLGLYAPTR RFGTRDEFRQ FITAAHNAGL NVLLDWVPGH FPSDDFGLAK FDGSELYEHH
     DPREGYHQDW NTLIYNFGRR EVSNFLAGNA LYWMERFGID GLRVDAVASM IYRDYSRKAG
     EWIPNEFGGR ENLEAISFLR YTNRVLGEEA DGSITVAEES TDYPGVTRPS EGGGLGFQYK
     WNLGWMHDTL DYMKQDPIYR RHHHNLMTFG MLYHYDENFV LPLSHDEVVH GKKSILDRMP
     GDAWQKFANL RAYYGWMWGF PGKKLLFMGN EFGQGREWNH DVSLDWHLLE GEDNWHNGVQ
     RLVRDLNKTY RHFPAMHQLD FDPQGFEWLV VDDFDNSVFV FVRRDSEGNE MIVASNFTPV
     TRENYRFGIN LPGGWREVLN TDSGHYHGSN TQNGTLVQSE PIASHKRDHS LSLTLPPLAT
     IWLVREDAE
//
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