ID A0A1I0HKJ3_9FIRM Unreviewed; 625 AA.
AC A0A1I0HKJ3;
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 {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN ORFNames=SAMN04489758_1516 {ECO:0000313|EMBL:SET83603.1};
OS Thomasclavelia cocleata.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=69824 {ECO:0000313|EMBL:SET83603.1, ECO:0000313|Proteomes:UP000198558};
RN [1] {ECO:0000313|Proteomes:UP000198558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1551 {ECO:0000313|Proteomes:UP000198558};
RA Varghese N., Submissions S.;
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}.
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};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR EMBL; FOIN01000051; SET83603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0HKJ3; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000198558; Unassembled WGS sequence.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
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-UniPathway.
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 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 {ECO:0000256|ARBA:ARBA00023277};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000198558};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 120..501
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 351
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 625 AA; 73471 MW; 2009AA4E0D415452 CRC64;
MLDDFLIHVF HKGNTLEAYK LFGAHFETNN HKKGVRFTVY APNARSVQVI GEFNDWDGKD
HYMERYTNGG IWTLFIPGIK EYTLYKYRIE TQNFATVDRA DPYAFYSELR PGTASRVYNI
ERFRWSDKKW LNNRTKNFDK PVNIYEANIG SWKMKKDFTD EEDGEFYTYE EMIDLLIPYL
VENNYTHLEL MPLTEFPFDG SWGYQVTGYY SITSRYGTPK EFMKFVNACH KAGIGVIMDF
VPAHYVKDGH GLYKFDGGFV YDYPDINQRY TEWDSVYFDV GRDEVRSFLM SSVGFLAEYF
HIDGIRFDAI SNLIYWKGNK EAGINDGAHE FMKRMNNHMK GYYPNVMLIA EDSSDFPGVT
KSPDVGGLGF DYKWDLGWMN DTLKYMKLNP VYRKYDHNLL TFSMAYFYGE NFILPFSHDE
VVHSKGTIID KIWGNNEQKF AQLKTLYTYM MIHPGKKLNF MGNELGEYKE WDEKVSLGWN
ILKYPIHDSF HNFIIKLNEI YQKYPCMYQQ DYGFDGFEWL VVDDSNQSVF AIERKDVKGN
SLIAVMNFTE NKHQGYMIPV NQSGNYKEIL NSDTDIYTGG NFINKRVIKT KKGFVLNKEY
YIPVNIAPFG SMIFEYRPTK SKNDK
//
