ID E1KTQ7_9BACT Unreviewed; 689 AA.
AC E1KTQ7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 67.
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=HMPREF9296_1876 {ECO:0000313|EMBL:EFL45133.1};
OS Prevotella disiens FB035-09AN.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=866771 {ECO:0000313|EMBL:EFL45133.1, ECO:0000313|Proteomes:UP000003610};
RN [1] {ECO:0000313|EMBL:EFL45133.1, ECO:0000313|Proteomes:UP000003610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB035-09AN {ECO:0000313|EMBL:EFL45133.1,
RC ECO:0000313|Proteomes:UP000003610};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:EFL45133.1}.
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DR EMBL; AEDO01000056; EFL45133.1; -; Genomic_DNA.
DR AlphaFoldDB; E1KTQ7; -.
DR STRING; 866771.HMPREF9296_1876; -.
DR eggNOG; COG0296; Bacteria.
DR Proteomes; UP000003610; 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; cd11321; AmyAc_bac_euk_BE; 1.
DR CDD; cd02854; E_set_GBE_euk_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; 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: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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 206..574
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 349
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 403
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 689 AA; 79576 MW; 4E33E9DF0643417F CRC64;
MIKKIQEKKS SAKKEAINNK VQLMGIAKND SYLAAYNEAI CGRHQNAVNK IKQLTNDGKQ
TLSDFANGYK YYGLHKANGK WIFREWAPNA TNIYLIGDFN QWQKTDEYKC NRITDSGDWE
LTIDEDKIKH GNLYKMQVSW CGGEGERIPA WADRVVQDEQ TKIFSAQVWF PDEEYTWKKK
SFKPTINPLL IYECHIGMGQ DAEKVGTYTE FKDNVLPRIV KAGYNAIQIM AIQEHPYYGS
FGYHVSSFFA ASSRFGTPEE LKALIDEAHA NGLAVIMDIV HSHAVKNELE GLGNLAGDPN
QYFYPGQRRE HPAWDSLCFD YGKNEVLHFL LSNCKYWIEE YHFDGFRFDG VTSMLYYSHG
LGESFGGYAD YFNGHQDDNA ICYLTLANCL IHEVNKHAIT IAEEVSGMPG LAAKFKDGGY
GFDYRMAMNI PDYWIKTIKE LSDENWKPSS IFWEIKNRRA DEKTISYCES HDQALVGDKT
IIFRLIDADM YWHFKKGDEN DRARRGIALH KMIRLATAAT INGGYLNFMG NEFGHPEWID
FPREGNGWSH KYARRQWNLV DNKELCYHYL GDFDQKMLET LKLEKDFNNT PLQEIWHNDS
DQILAFSRND LIFIFNFSPN HSFSDYGFLV PEGTYNVVLN TDSWEFGGNG FVDEKINHTT
ITDPLYKEQK KGWLKVYIPA RSALVLKKK
//
