ID Q9XGA8_SOLTU Unreviewed; 882 AA.
AC Q9XGA8;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 24-JAN-2024, entry version 96.
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=SBE II {ECO:0000313|EMBL:CAB40748.1};
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:CAB40748.1};
RN [1] {ECO:0000313|EMBL:CAB40748.1}
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; AJ011890; CAB40748.1; -; mRNA.
DR AlphaFoldDB; Q9XGA8; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR UniPathway; UPA00152; -.
DR ExpressionAtlas; Q9XGA8; 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:CAB40748.1}; Plastid {ECO:0000256|ARBA:ARBA00023234};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAB40748.1}.
FT DOMAIN 363..723
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 68..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 506
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 561
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 882 AA; 100864 MW; FB50F9AF7825EB87 CRC64;
MVYTLSGVRF PTVPSVYKSN GFSSNGDRRN ANVSVFLKKH SLSRKILAEK SSYNSEFRPS
TVAASGKVLV PGTQSDSSSS STDQFEFTET SPENSPASTD VDSSTMEHAS QIKTENDDVE
PSSDLTGSVE ELDFASSLQL QEGGKLEESK TLNTSEETII DESDRIRERG IPPPGLGQKI
YEIDPLLTNY RQHLDYRYSQ YKKLREAIDK YEGGLEAFSR GYEKMGFTRS ATGITYREWA
LGAQSAALIG DFNNWDANAD IMTRNEFGVW EIFLPNNVDG SPAIPHGSRV KIRMDTPSGV
KDSIPAWINY SLQLPDEIPY NGIHYDPPEE ERYIFQHPRP KKPKSLRIYE SHIGMSSPEP
KINSYVNFRD EVLPRIKKLG YNALQIMAIQ EHSYYASFGY HVTNFFAPSS RFGTPDDLKS
LIDKAHELGI VVLMDIVHSH ASNNTLDGLN MFDCTDSCYF HSGARGYHWM WDSRLFNYGN
WEVLRYLLSN ARWWLDAFKF DGFRFDGVTS MMYIHHGLSV GFTGNYEEYF GLATDVDAVV
YLMLVNDLIH GLFPDAITIG EDVSGMPTFC IPVQEGGVGF DYRLHMAIAD KRIELLKKRD
EDWRVGDIVH TLTNRRWSEK CVSYAESHDQ ALVGDKTIAF WLMDKDMYDF MALDRPSTSL
IDRGIALHKM IRLVTMGLGG EGYLNFMGNE FGHPEWIDFP RAEQHLSDGS VIPGNQFSYD
KCRRRFDLGD AEYLRYRGLQ EFDRPMQYLE DKYEFMTSEH QFISRKDEGD RMIVFEKGNL
VFVFNFHWTK SYSDYRIACL KPGKYKVALD SDDPLFGGFG RIDHNAEYFT FEGWYDDRPR
SIMVYAPCKT AVVYALVDKE EEEEEEEEEE VAAVEEVVVE EE
//
