ID Q9XGA7_SOLTU Unreviewed; 836 AA.
AC Q9XGA7;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 24-JAN-2024, entry version 93.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
DE Flags: Fragment;
GN Name=SBE II {ECO:0000313|EMBL:CAB40747.1};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EMBL:CAB40747.1};
RN [1] {ECO:0000313|EMBL:CAB40747.1}
RP NUCLEOTIDE SEQUENCE.
RA Jobling S.A., Schwall G.P., Westcott R.J., Sidebottom C.M., Debet M.,
RA Gidley M.J., Jeffcoat R., Safford R.;
RT "A minor form of starch branching enzyme in potato (Solanum tuberosum L.)
RT tubers has a major effect on starch structure; cloning and characterisation
RT of multiple forms of SBE II.";
RL Submitted (OCT-1998) 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; AJ011889; CAB40747.1; -; mRNA.
DR AlphaFoldDB; Q9XGA7; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR UniPathway; UPA00152; -.
DR ExpressionAtlas; Q9XGA7; baseline.
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:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:CAB40747.1}; Plastid {ECO:0000256|ARBA:ARBA00023234};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAB40747.1}.
FT DOMAIN 318..678
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 23..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 461
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 516
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAB40747.1"
SQ SEQUENCE 836 AA; 95819 MW; 0F8AEA5B6A5AD0F7 CRC64;
ILAEKSSYNS EFRPSTVAAS GKVLVPGTQS DSSSSSTNQF EFTETSPENS PASTDVDSST
MEHASQIKTE NDDVEPSSDL TGSVEELDFA SSLQLQEGGK LEESKTLNTS EETIIDESDR
IRERGIPPPG LGQKIYEIDP LLTNYRQHLD YRYSQYKKLR EAIDKYEGGL EAFSRGYEKM
GFTRSATGIT YREWAPGAQS AALIGDFNNW DANADIMTRN EFGVWEIFLP NNVDGSPAIP
HGSRVKIRMD TPSGVKDSIP AWINYSLQLP DEIPYNGIYY DPPEEERYIF QHPRPKKPKS
LRIYESHIGM SSPEPKINSY VNFRDEVLPR IKKLGYNALQ IMAIQEHSYY ASFGYHVTNF
FAPSSRFGTP DDLKSLIDKA HELGIVVLMD IVHSHASNNT LDGLNMFDGT DSCYFHSGAR
GYHWMWDSRL FNYGNWEVLR YLLSNARWWL DEFKFDGFRF DGVTSMMYTH HGLSVGFTGN
YEEYFGLATD VDAVVYLMLV NDLIHGLFPD AITIGEDVSG MPTFCIPVQD GGVGFDYRLH
MAIADKWIEL LKKRDEDWRV GDIVHTLTNR RWSEKCVSYA ESHDQALVGD KTIAFWLMDK
DMYDFMALDR PSTSLIDRGI ALHKMIRLVT MGLGGEGYLN FMGNEFGHPE WIDFPRAEQH
LSDDSVIPGN QFSYDKCRRR FDLGDAEYLR YRGLQEFDRA MQYLEDKYEF MTSEHQFISR
KDEGDRMIVF EKGNLVFVFN FHWTKSYSDY RIGCLKPGKY KVALDSDDPL FGGFGRIDHN
AEYFTFEGWY DDRPRSIMVY APCRTAVVYA LVDKEEEEEE EEEEVAVVEE VVVEEE
//
