ID   W9R904_9ROSA            Unreviewed;       959 AA.
AC   W9R904;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=L484_012478 {ECO:0000313|EMBL:EXB63288.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB63288.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) 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   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004727}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC       {ECO:0000256|ARBA:ARBA00004602}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR   EMBL; KE344484; EXB63288.1; -; Genomic_DNA.
DR   RefSeq; XP_010096123.1; XM_010097821.1.
DR   AlphaFoldDB; W9R904; -.
DR   STRING; 981085.W9R904; -.
DR   eggNOG; KOG0470; Eukaryota.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000030645; Unassembled WGS sequence.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
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:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
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; 2.
DR   InterPro; IPR006048; A-amylase/branching_C.
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:SF4; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME 3, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF02922; CBM_48; 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   Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW   Plastid {ECO:0000256|ARBA:ARBA00023234};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          384..745
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          44..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   959 AA;  110263 MW;  15D7B43A51C076A4 CRC64;
     MATSLSFPTK FSLHPNSSVF VFQSPNGPKR IRFPKKINKV LCSATEQPKQ QQQKQQRWQT
     NKKKKSDSDA EKGIDPVGFL TKTGISHRQF AQFLRERHKA LKDLKDEIFN RHVNLRDLAS
     GFEILGMHRH PEHRVDYMEW APGARYCALV GDFNGWSQTD NAAREGHLGH DDYGYWFIIL
     EDKLREGENP DELYFQQYNY VEDYDKGDSG VPIEEIFKKA NDEYWEPGED RFLNHRFEVP
     AKLYEQIFGP NGPQTLEELG EIPDAETRYK EWKEQHKDDP PSNSPCYDVI DNGKEYDIFN
     VVVDPVSREK FKSKKPPLAY WFETRKGRKA WLKKYTPGIP HGSKYRVYFN TPNGPLERVP
     AWATYVQPEG NQAFAIHWEP PPEDAYKWRN TSPKVPKSLR IYECHVLPHV KEAGYNAIQF
     IGVVEHKDYF TVGYRVTNHY AVSSRFGTPD DFKRLVDEAH GLGLLVFLDI VHSYSAADEM
     VGLSLFDGSN DCYFHTGKRG HHKYWGTRML KYGDLDVLHF LLSNLNWWVV EYQIDGFQFH
     SLSSMMYTHN GFASFTGDLE EYCNQSVDRE ALLYLILANE ILHGLHPNII TIAEDATYYP
     GLCEPTSQGG LGFDYYVNLS VPDMWSSFLQ NVPDHEWSMS KIVSTLTGNK QYTDKMLVYA
     ENHNQSISGG HSFAEILLGE IMKDSDATKE SLLRGCSLLK MIRLITFTIG GRAYLNFMGN
     EFGHPERVEF PMSSNNFSFS LANRRWDLLA KEGVHRNLFI FDKDLMNLDE KGRILSGVQP
     NIHHVNDTTK LNNRKSSFKQ PFNSWTASRR GVKGCLRPAQ PQEHVSKGVG HLPSLNCKMY
     AKPNQVIAYM RGPLLFIFNF HPTDSYEGYG VGVEEAGEYQ LILNTDEVEY GGQGLVKEHQ
     HTRKTFSKRV DALRHCLEVP LPSRTAQVGF LFSFRVFGIY APELFTIGKL SLNVLSFEN
//