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Database: UniProt
Entry: A0A1I6LCL6_9FIRM
LinkDB: A0A1I6LCL6_9FIRM
Original site: A0A1I6LCL6_9FIRM 
ID   A0A1I6LCL6_9FIRM        Unreviewed;       746 AA.
AC   A0A1I6LCL6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN05661086_03202 {ECO:0000313|EMBL:SFS01028.1};
OS   Anaeromicropila populeti.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaeromicropila.
OX   NCBI_TaxID=37658 {ECO:0000313|EMBL:SFS01028.1, ECO:0000313|Proteomes:UP000199659};
RN   [1] {ECO:0000313|EMBL:SFS01028.1, ECO:0000313|Proteomes:UP000199659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=743A {ECO:0000313|EMBL:SFS01028.1,
RC   ECO:0000313|Proteomes:UP000199659};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOYZ01000015; SFS01028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6LCL6; -.
DR   STRING; 37658.SAMN05661086_03202; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000199659; 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; 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; 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:UP000199659};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00685}.
FT   DOMAIN          257..620
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        417
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        470
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT                   ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   746 AA;  86110 MW;  684FAD63B2E78052 CRC64;
     MDQRLMDFIN KDQYEELQKG INNCPKKLLG LHKISGGYVL VVYRPYAKSV KATDVSGCSR
     YYLKPIDDAG TFGAFFEELP FENYLLEIEY GVNDIVITED PYSFSSEIGE LDLHLFGEGK
     HYEIYNKLGA HPVVRNSVEG VSFAVWAPHA RSVSVIGDFN MWDGRLHPMN LISSSGIYEL
     FIPRVQPGAI YKYQVVTRSG EVLHKSDPYA NCSELRPNNA SVVADITNYY WQDDSWMKQR
     TQKARVDYLK EPINIYEVHL GSWKKHNDND DNGFYNYREL AHELADYVVD MGYTHIELMG
     IAEYPFDGSW GYQVTGYYAP TRRYGTPQDF MYFIDYMHQK GISIILDWVP AHFPKDAHGL
     ARFDGEALFE HPDSRRGEHP HWGTYIFNYG KKEVENFLLA NVLFWIKQYH IDGIRVDAVA
     SMLYLDYGKQ DGEWLPNENG GRENYDAILL MQHINEVVEK DYPGVLVIAE ESTAWAGVTA
     PVDMKGLGFH FKWNMGWMND FLEYMKLDPY FRQFNHNRLT FSLMYAYSEN FIQVLSHDEV
     VHGKCTLLNK MPGEDFDKFA NLRTAYGFMY GHPGKKLLFM GQEFAQLREW SEARSLDWYL
     LQEEKHQQMQ HYVKTLNKLY LKNSAFYAND AEQIGFEWID CSDAQSSIIS FIRRGNSSKD
     QLLFVCNFTP VEKTEFTVGV PCPGNYTEVL NSDALEFGGQ GKIIGGSVHA VKKSCNGKTY
     SITFTLPPLS IVVFHYHYHS GKKKKR
//
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