ID A0A183MSY0_9TREM Unreviewed; 644 AA.
AC A0A183MSY0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-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};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0001915601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0001915601-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; A0A183MSY0; -.
DR STRING; 48269.A0A183MSY0; -.
DR WBParaSite; SMRZ_0001915601-mRNA-1; SMRZ_0001915601-mRNA-1; SMRZ_0001915601.
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:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR CDD; cd11321; AmyAc_bac_euk_BE; 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; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
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 PIRSF; PIRSF000463; GlgB; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 158..507
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 296
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 351
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 644 AA; 74995 MW; C8409E2430965867 CRC64;
LLQLDPWLEP FKHEIKRRVT RNSGFMYVMT DQYTAKNGLQ GRKNYDWQEF THPFKNVGFG
KWELTIPSAN GSPVIKHLSK IKLLVVAHDG RRLDRLSPWA PYVKCFEGNI IYDQLLYNPS
ERYLLKYPHP PRPKSLRIYE CHIGISSSEP VVASYSHFKD NILPRIKDLG YNAIQIMALM
EHAYYASFGY QVTSFFAASS RFGTPEELRA MVDEAHRLGI VVLLDVVHSH ASKNTNDGLN
QFDGTNACYF HDLGRGTHEL WDSRLFNYTE LEVLRFLMSN LRWWIEEYGF DGFRFDGVMS
MLYHHHGLMT NFSGHYGEYF GLSVDTESFT YLMLANHFLH EKYPFIITIA EEVSGMPTLC
RPVSEGGGGF DYRLAMAIPD KWIELLKKYK DEDWNMGNLV HTLTNRRYGE PNIAYAECHD
QALVGDKTLS FWLMDKEMYF SMSTLSPPNL IIDRGIALHK LIRFITHTLG GEGYLNFMGN
EFGHPEWLDF PRAGNNSSYH YARRQWNLVD DPLLRYKYLN NFDRAMQHLE EKYGWLAYVS
RKNEGDKVIA FERAGVLFAF NFHPTQSFTD YKIGVDTPGQ YHIVLDSDQE EFGGFKRIDQ
SVDVFTRNEP WDNRRNCVFL YLPSRTCMAL ALERENCDYK SEIA
//