ID A0A2R5HJL5_9LACT Unreviewed; 648 AA.
AC A0A2R5HJL5;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN Name=glgB {ECO:0000313|EMBL:GBG96818.1};
GN ORFNames=NtB2_00942 {ECO:0000313|EMBL:GBG96818.1};
OS Lactococcus termiticola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=2169526 {ECO:0000313|EMBL:GBG96818.1, ECO:0000313|Proteomes:UP000245021};
RN [1] {ECO:0000313|EMBL:GBG96818.1, ECO:0000313|Proteomes:UP000245021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NtB2 {ECO:0000313|EMBL:GBG96818.1,
RC ECO:0000313|Proteomes:UP000245021};
RA Noda S., Aihara C., Yuki M., Ohkuma M.;
RT "Draft Genome Sequence of Lactococcus sp. Strain NtB2 (JCM 32569), Isolated
RT from the Gut of the Higher Termite Nasutitermes takasagoensis.";
RL Genome Announc. 6:e00445-18(2018).
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 -!- 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:GBG96818.1}.
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DR EMBL; BFFO01000005; GBG96818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R5HJL5; -.
DR OrthoDB; 9800174at2; -.
DR Proteomes; UP000245021; 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 Reference proteome {ECO:0000313|Proteomes:UP000245021};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 184..544
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 319
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 373
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 648 AA; 74472 MW; E2EBE51C7203CFC6 CRC64;
MNILEYDPYL EPFKEDLSKR LFDFARTKKR LLGVDGRLTD FANGYKYFGF QQEADHWTFR
EWAPNVEAAY LVGDFNDWDG KSHELKAGYG GVWELVVPGK LPVGSKVKVQ LMVDGKPLYR
VPSYMNYVVQ NERYEMDGVI YEPSYQFKHQ APALGKEAPL IYEAHIGIST EEYRINSYRE
FREDVLPRIK ADGYNTIQLM AIMEHPLYAS FGYQVSNFYA ASSRFGTPDE LMALIDEAHG
MGIRVLLDVV HSHAVKNVGD GLNLFDGTTS QYFHEGERGE HREWNTKLFN YGKDEVIHFL
LSNLKFWLDV YRFDGFRFDG VTSMLYHDHG LGTAFTDYSK YFSLNTDVEA VTYLMLANEL
IHEFRPGATT IAEDMSAMPG MALPISDGGI GFDYRLSMGI PDYWIKQFKK KTDDQLDLME
LWWELTIRRP GEKNIGYAES HDQALVGDKT LMMWLADAEI YTKMDIHSQS LVIDRAIALH
KLVRLVTFSL AGEGYLNFMG NEFGHPEWLD FPREGNGDDY QHARRQWSLA ENEGLRFKYL
LAFDQAMIAL EHDHDFLAKS NEVQQKWVKN EDKLLAYQKG ELLFVFNFHP TEMKQVSFAS
GPVELIFDTD DAKFGGFGPR SSFNYEAGSF SAELAARSAM VFKLTSKD
//
