ID   Q9XGB2_WHEAT            Unreviewed;       865 AA.
AC   Q9XGB2;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=sbe1 {ECO:0000313|EMBL:CAB40980.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EMBL:CAB40980.1};
RN   [1] {ECO:0000313|EMBL:CAB40980.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=10527426; DOI=10.1023/A:1006286807176;
RA   Baga M., Glaze S., Mallard C.S., Chibbar R.N.;
RT   "A starch-branching enzyme gene in wheat produces alternatively spliced
RT   transcripts.";
RL   Plant Mol. Biol. 40:1019-1030(1999).
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; AJ237897; CAB40980.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XGB2; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   UniPathway; UPA00152; -.
DR   ExpressionAtlas; Q9XGB2; baseline and differential.
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   GO; GO:0005983; P:starch catabolic process; IEA:UniProt.
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; 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:SF2; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME, 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   Glycosyltransferase {ECO:0000313|EMBL:CAB40980.1};
KW   Plastid {ECO:0000256|ARBA:ARBA00023234};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAB40980.1}.
FT   DOMAIN          300..667
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   865 AA;  97503 MW;  64D980B0F0ABAA22 CRC64;
     MLCLTASSSP SPSPSLPPRP SRPAADRPGP GISVSHSGSS FLFFSFVSGL RSASRRFPDA
     MPRAQGGGNV RLSAVPAPSS LRWSWPRKAK SKFSVPVSAP RDYTMATAED GFGDLPIYDL
     DPKFAGFKDH FSYRMKKYLE QKHSIEKYEG GLEEFSKGYL KFGINTENDA TVYREWAPAA
     KDAQLIGDFN NWNGSGHRMT KDNFGVWSIR ISHVNGKPAI PHNSKVKFRF HRGDGLWVDR
     VPAWIRYATF DASKFGAPYD GVHWDPPTGE RYVFKHPRPR KPDAPRIYEA HVGMSGEKPE
     VSTYREFADN VLPRIKANNY NTVQLMAIME HSYYASFGYH VTNFFAVSSR SGTPEDLKYL
     VDKAHSLGLR VLMDVVHSHA SSNMTDGLNG YDVGQNTQES YFHTGERGYH KLWDSRLFNY
     ANWEVLRYLL SNLRYWMDEF MFDGFRFDGV TSMLYNHHGI NMSFAGNYKE YFGLDTDVDA
     VVYMMLANHL MHKILPEATV VAEDVSGMPV LCRSVDEGGV GFDYRLAMAI PDRWIDYLKN
     KDDLEWSMSA IAHTLTNRRY TEKCIAYAES HDQSIVGDKT MAFLLMDKEM YTGMSDLQPA
     SPTIDRGIAL QKMIHFITMA LGGDGYLNFM GNEFGHPEWI DFPREGNNWS YDKCRRQWSL
     SDIDHLRYKY MNAFDQAMNA LDDKFSFLSS SKQIVSDMNE EKKIIVFERG DLVFVFNFHP
     SKTYDGYKVG CDLPGKYKVA LDSDALMFGG HGRVAHDNDH FTSPEGVPGV PETNFNNRPN
     SFKVLSPPRT CVAYYRVEEK AEKPKDEGAA SWGKAAPGYI DVEATRVKDA ADGEATSGSK
     KASTGGDSSK KGINFVFGSP DKDNK
//