ID   A0A0R3S3D5_9BILA        Unreviewed;       708 AA.
AC   A0A0R3S3D5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE            EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000927001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000927001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A0R3S3D5; -.
DR   STRING; 1147741.A0A0R3S3D5; -.
DR   WBParaSite; EEL_0000927001-mRNA-1; EEL_0000927001-mRNA-1; EEL_0000927001.
DR   Proteomes; UP000050640; Unplaced.
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          193..530
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        356
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        411
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   708 AA;  82308 MW;  49A1399F4CC74822 CRC64;
     MSGSGNRPPR LDNLLKLDGY LWNYQNEICR RYGVFLDYSK KIEECGGWET FTTAYREYGV
     LVMRDKSVHC LEWAPGADAL SLVGDFNSWN TESHPYKKLE YGKWELIIPA DKDGNCPIKH
     GSIIKVAVKK DNVFHFKLSP WAHYVTRPKE TTVYHMPFYN PPESERYHFK HPKPAKPESL
     RIYEAHVGIS SLEGKVNSYQ NFANDVIPRI KKQGYNTIQL MAIMEHVYYA SFGYQVTSFF
     APSSRFGTPE DLKYLVDKSH EAGILILLDV VHSHASKNVD DGLNEWDGTQ NSYFHDNNRG
     YHSLWDSRLF DYTQKVFETF VKTFFELEFW VETLRFLLSN LRWWIEEYGF DGFRFDGVTS
     MIYHSHGIAD ALDGGYDMYF GLNADTDSLV YLMLANSFLH RKFPNIITIA EEVSGMPALC
     RPVEEGGQGF DYRLAMAAPD LWIKLLKHFS DENWDISNLV FTLENRRYAE KHIAYAESHD
     QALVGDKTIA FWLMDKADYV LEMYDFMSDT TPLTPIIERG IALHKMIRLI TYALGGEAWL
     NFIGNEFGHP EWLDFPRVGN NESFHYCRRQ WNLADNELLR YKYLNNFDRA MNKLEEKYLF
     LSRGPAYTSW KHQDDKVIAF ERAGLLFVFN FHTHKSFSDY KIGIEVAGEY ALALSTDDTE
     FGGFNRLDKS QHYLTFPEGY AGRRNHLYVY IPCRVAIVLE KVGERPAS
//