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Database: UniProt
Entry: A0A081NLX8_9GAMM
LinkDB: A0A081NLX8_9GAMM
Original site: A0A081NLX8_9GAMM 
ID   A0A081NLX8_9GAMM        Unreviewed;       735 AA.
AC   A0A081NLX8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=GZ78_05800 {ECO:0000313|EMBL:KEQ19451.1};
OS   Endozoicomonas numazuensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Endozoicomonadaceae; Endozoicomonas.
OX   NCBI_TaxID=1137799 {ECO:0000313|EMBL:KEQ19451.1, ECO:0000313|Proteomes:UP000028073};
RN   [1] {ECO:0000313|EMBL:KEQ19451.1, ECO:0000313|Proteomes:UP000028073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25634 {ECO:0000313|EMBL:KEQ19451.1,
RC   ECO:0000313|Proteomes:UP000028073};
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:KEQ19451.1}.
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DR   EMBL; JOKH01000001; KEQ19451.1; -; Genomic_DNA.
DR   RefSeq; WP_034833312.1; NZ_JOKH01000001.1.
DR   AlphaFoldDB; A0A081NLX8; -.
DR   STRING; 1137799.GZ78_05800; -.
DR   eggNOG; COG0296; Bacteria.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000028073; 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:UP000028073};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          255..615
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        464
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   735 AA;  83845 MW;  5A373C5192BDD01E CRC64;
     MPNSVEPLIG HLLDCRCAEP FNLLGFHERP EGSHERTGNS GLLLRVWRPD ASNVSVITFT
     SGEAIGEMVQ VAPGLFELLL SECCSVFLYQ LVVTNKDHQS YTLVDPYQFQ SYSLSHFHRE
     PYRNYRYMGA HLVSLHPEPK VTIDGVIFRV YAPNARSVSL VGSFNGWDGR MHPMASSDDG
     IWRLFIPGVK AGDLYKYEIR SQQGDLLPHK ADPYGYYAEQ PPGNASIVYD HLDYEWEDSR
     WKHHACLDRP VSIYEVHLGS WRKEQGKNLT YKTLAEQLIP YVVDMGFTHI ELMPPMEHPF
     TGSWGYQPVG LFAPTSRFGN PDDFKAFIDS CHQAGIGVIL DWVPAHFPSD SHGLGRFDGA
     ALYEYADPKR GWHPDWQTHI YDYGKPEVKE FLISNAMYWL DRFHLDGVRV DAVASMLYLD
     YSRSEGEWEP NQLGGNEHIE AVQFLKELNE TLYLHYPDQV SIAEESTSWP KVSMPTYDGG
     LGFGYKWNMG WMHDTLDYMT RDPIHRAHNH WEIMQSMTYH YSEHFILALS HDEVVHGKGS
     LLGKMPGDEW QKYANLRAYL GFMFGHPGKK LLFMGAEIGS VREWDHEGQL DWELLNKNNY
     SQGLSQLVKE LNHLYKSYPA LYKSDYDQNG FAWVVADDQQ QSVFAFIRKS FSGSPVLVIA
     NMTPEVRQDY RVGVPVKGVW KEVLNSDGQC FGGSGVANSK SLYTEHYHTH GYDCSLVVTL
     PPLATLFLVP DSCAI
//
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