ID A0A1G1SYD8_9BACT Unreviewed; 683 AA.
AC A0A1G1SYD8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=BEN47_17380 {ECO:0000313|EMBL:OGX83620.1};
OS Hymenobacter lapidarius.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1908237 {ECO:0000313|EMBL:OGX83620.1, ECO:0000313|Proteomes:UP000176294};
RN [1] {ECO:0000313|EMBL:OGX83620.1, ECO:0000313|Proteomes:UP000176294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8643 {ECO:0000313|EMBL:OGX83620.1,
RC ECO:0000313|Proteomes:UP000176294};
RA Sedlacek I., Kralova S., Kyrova K., Maslanova I., Stankova E., Vrbovska V.,
RA Nemec M., Bartak M., Svec P., Busse H.-J., Pantucek R.;
RT "Hymenobacter coccineus sp. nov., Hymenobacter lapidarius sp. nov. and
RT Hymenobacter glacialis sp. nov., isolated from Antarctic soil.";
RL Submitted (AUG-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:OGX83620.1}.
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DR EMBL; MDZB01000129; OGX83620.1; -; Genomic_DNA.
DR RefSeq; WP_070729170.1; NZ_MDZB01000129.1.
DR AlphaFoldDB; A0A1G1SYD8; -.
DR STRING; 1908237.BEN47_17380; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000176294; 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 174..575
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 404
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 683 AA; 76898 MW; 50B7DB17A45EA3B9 CRC64;
MAKTTPIAPA TPKASRLAPL ALVKNDAYLA PFEPVLRQRQ ARLQARLAEI KQHHGSLLNY
ATAHQQLGLH HSAGRGGYVY REWAPGAEGL FLVGDFNGWD RQANPLQLLD FGVWEVFLPD
AEYKSRLTHG SRYKVHVVAN GQGKDRLPAT LRRTVQDDDT KDFAGQIWQP ETPFAWTDQK
FKPATAVPEP LIYEAHVGMA TEEGRVGTYR EFADHILPRI AAGGYNTIQL MAVQEHPYYG
SFGYHVANLF AASSRFGTPE DLKYLINEAH RRDIAVLLDI VHSHAVKNEA EGLANFDGSG
NLYFHKGERG NHPGWDSKLF DYGRPEVQQF LLSNLRFWLE EYHFDGFRFD GVTSMLYHHH
GEGVAFVGYD NYFGPSADED AILYLQLATT LAHEFKKGSI LVAEDMSGLP GLCRPIKEGG
VGFDYRLAMG IPDFWIKLLK HTPDENWPLG DLWHTLTNRR AGEKTIAYAE SHDQALVGDK
TLAHWLFDAA IYSHMHTADG DPGAARALAL HKLIRLLTLA AGGEGYLTFI GNEFGHPEWV
DFPRAGNDWS YQFARRQWSL GDNPDLKFSQ MGAFDKAMVQ LARQRHLLAA GPATLLKHDE
ENKVLAFERA GLVFIINFHV EQSLTDYRFW VTEEGKYRVV LSSDNSRFGG FDRPDEAFEY
ETFEHQLSLY VPSRVALVVE VGS
//
