ID   A0A183QSH5_9TREM        Unreviewed;       684 AA.
AC   A0A183QSH5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE            EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
OS   Schistosoma rodhaini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0000662301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SROB_0000662301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) 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; A0A183QSH5; -.
DR   STRING; 6188.A0A183QSH5; -.
DR   WBParaSite; SRDH1_38500.1; SRDH1_38500.1; SRDH1_38500.
DR   WBParaSite; SROB_0000662301-mRNA-1; SROB_0000662301-mRNA-1; SROB_0000662301.
DR   Proteomes; UP000050792; 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          205..554
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        343
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        398
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   684 AA;  79645 MW;  825D484F9E67F2E4 CRC64;
     MSYTAEEIEA VNVPNIQNLL QLDPWLEPYK HEIKRRYKCF LDHMKWINDV CGLEEFTQGY
     KEFGVHVRDD GSIYCKEWAP GAKEMYLRGD FNDWQEFTHP FKNVGFGKWE LTIPSANGSP
     VINHLSKIKL LVVAQDGRRL DRLSPWAPYV KCFEGNIIYD QLLYSPPERY QLKYPHPPRP
     KSLRIYECHI GISSSEPVVA SYSHFKDNIL PRIKDLGYNA IQIMALMEHA YYASFGYQVT
     SFFAASSRFG TPEELRAMVD EAHRLGIVVL LDVVHSHASK NTNDGLNQFD GTNACYFHDL
     GRGTHELWDS RLFNYTELEV LRFLMSNLRW WIEEYGFDGF RFDGVMSMLY HHHGLMTNFS
     GHYGEYFGLS VDTESFTYLM LANHFLHEKY PFIITIAEEV SGMPTLCRPV SEGGGGFDYR
     LAMAIPDKWI ELLKKYKDED WNMSNLVHTL TNRRYGEPNI AYTECHDQAL VGDKTLSFWL
     MDKEMYFSMS TLSPPNLIID RGIALHKLIR FITHTLGGEG YLNFMGNEFG HPEWLDFPRA
     GNNSSYHYAR RQWNLVDDPL LRYKYLNNFD RAMQHLEERY GWLAAPQAYV SRKNEGDKVI
     AFERAGVLFV FNFHPTQSFA DYKIGVETPG QYHIVLDSDQ EEFGGFKRID QSVDVFTRNE
     PWDNRRNCVF LYLPSRTCMA LALQ
//