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Database: UniProt
Entry: A0A081N8J3_9GAMM
LinkDB: A0A081N8J3_9GAMM
Original site: A0A081N8J3_9GAMM 
ID   A0A081N8J3_9GAMM        Unreviewed;       715 AA.
AC   A0A081N8J3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-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   ORFNames=GZ77_10785 {ECO:0000313|EMBL:KEQ14766.1};
OS   Endozoicomonas montiporae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Endozoicomonadaceae; Endozoicomonas.
OX   NCBI_TaxID=1027273 {ECO:0000313|EMBL:KEQ14766.1, ECO:0000313|Proteomes:UP000028006};
RN   [1] {ECO:0000313|EMBL:KEQ14766.1, ECO:0000313|Proteomes:UP000028006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24815 {ECO:0000313|EMBL:KEQ14766.1,
RC   ECO:0000313|Proteomes:UP000028006};
RA   Neave M.J., Apprill A., Voolstra C.R.;
RT   "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL   Submitted (JUN-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEQ14766.1}.
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DR   EMBL; JOKG01000002; KEQ14766.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A081N8J3; -.
DR   eggNOG; COG0296; Bacteria.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000028006; Unassembled WGS sequence.
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:UP000028006};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          240..617
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        397
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        450
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   715 AA;  81961 MW;  5E163B9CA82D83D7 CRC64;
     MLDRAQVSCP FDYLGIQPHD SGKGLVVRFW NPNAVSATLI QLPRKTVIST MKCLSPGLFE
     WHLPRRKKAF NYVIKAVMSD GRQEEIVDPY QFGEYVLKQH DIEPSALYRH LGAHLHEHAV
     SASVSISGTL FKVYAPNARS VSVVGSFNDW DGRIHPMASA DDGIWRLFIP GVEEQALYKF
     ELHDQQGNLL PLKADPFGRY SEQYPGLASI VDRPQRYQWR DDDWLKHRTQ MHSKPMSVYE
     VHPGSWKRHS DGRPLSYREL AEQLIPYVRK MGFTHIELMP VNEHPYFESW GYQPVGLFAP
     TSRYGSPDDF KFFVDRCHQA GIGVILDWVP AHFPEDKHGL ARFDGTALYE YEDTSRGFHP
     DWHTLIYNFG SGWVQDFLIS SALFWLDEFH IDGLRVDAVA SMLYLDYSRQ AGEWKPNRYG
     GNEHLEAVTF LQRLNTLAGR YFPDCMTIAE ESTSWGGVSR PVNEGGLGFG FKWNMGWMHD
     SLEYMQRLPE HRCYHHTELS FSMVYAYSEN FVLSLSHDEV VHGKGTILDR MPGDAWQKMA
     NLRAYYGLMF AHPGKKLLFM GNELASTSEW DVNSSLQWSL LEQKEHAGIQ TLVKDLNVVY
     RSVPALYELD HSRDGFRWLI IDDHAQSVYA WLRRDKAGNP VVVICNMTPV VRNHYRVGVP
     ESKGWCELIN TDDLRYGGSG VGDDQYNSEM VPSHGYKQSF SLTLPPLSTL ILQGI
//
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