ID A0A1M3BSH7_9BACT Unreviewed; 590 AA.
AC A0A1M3BSH7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=BGO17_00580 {ECO:0000313|EMBL:OJU87483.1};
OS Candidatus Saccharibacteria bacterium 49-20.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1895829 {ECO:0000313|EMBL:OJU87483.1, ECO:0000313|Proteomes:UP000184370};
RN [1] {ECO:0000313|EMBL:OJU87483.1, ECO:0000313|Proteomes:UP000184370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=49-20 {ECO:0000313|EMBL:OJU87483.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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:OJU87483.1}.
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DR EMBL; MKSN01000001; OJU87483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3BSH7; -.
DR STRING; 1895829.BGO17_00580; -.
DR Proteomes; UP000184370; 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:InterPro.
DR CDD; cd11325; AmyAc_GTHase; 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; 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 PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 123..471
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 281
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 326
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 590 AA; 66051 MW; 486F913A1BA135E6 CRC64;
MGHRTNKHLG ATVHDKGVDF AVWAPFAKAV SLLHWQEFDW KEIPMASDGE GYWFIKDVDA
AAGQTYKYRI TTQHDEILEK NDPYARQLTD SDSGSSVIVA HDFDWQGADE FSPVEKVKAV
IYELHVGTFN KPDASTTGTF ATVVEKLDYL KELGINTIEL MPVTSMAMSH GWGYAPNHIF
SIEAAYGGRH GLLELVKASH EKGISVILDV VYNHFYLETD LWQYDGWSEN NRGGIYFFND
ERGDTPWGGR PDYGRPEVRQ FILDNVAMWF NEYKVDGLRV DSTIYMRNTD GNNDKHDLDI
PEAWTLMNEV NELAHKIKPG ALMIAEDNST NSGIVTKEGM GFDAQWEVGF PHVIRDSLGI
THNDSQPALQ GVEWALGHSY TGSAFDKVIF GDSHDTAANG SSRLNEATTP GNAESLSARQ
RVLLASAITL TAPGIPMLLQ GQEFMQEGAF NEWQMLEWGK TEQFSGIVDA HKHLIDLRLN
TYDNTRGLVG EHTTLLHRDD IHNVLAYLRS DKGGPLDDTV VIVNFGAEKF KNYEIPFPSA
GEWIVRFNSS WKGYNVDFHE TNIRSVHVGE DLKASLAFSG YSALILSKDS
//
