ID Q948N7_IPOBA Unreviewed; 868 AA.
AC Q948N7;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 81.
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:BAB64912.1};
OS Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=4120 {ECO:0000313|EMBL:BAB64912.1};
RN [1] {ECO:0000313|EMBL:BAB64912.1}
RP NUCLEOTIDE SEQUENCE.
RA Kimura T., Saito A.;
RT "Ipomoea batatas mRNA for starch branching enzyme II.";
RL Submitted (SEP-2001) 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; AB071286; BAB64912.1; -; mRNA.
DR AlphaFoldDB; Q948N7; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR UniPathway; UPA00152; -.
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:BAB64912.1}; Plastid {ECO:0000256|ARBA:ARBA00023234};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAB64912.1}.
FT DOMAIN 363..674
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 124..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..152
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 868 AA; 99349 MW; A64A6637DFF7874D CRC64;
MVYTLSGLRL PAVAPVYKHL GSTSHADRRN TNPSLSLKRN SFSSWKIFAR NTSYESEPSS
FRVAASEKVL VPGGEGEGSS FPTDQLEVAE ALSEDTQVSA DVDNVKMEEN SNSESNVDFV
KVASDSKESV QEQDHTSSLQ FEEDGNVEVS QKPETLDDIS AESEMVKKRA IPPPGLGQRI
YEIDPLLKNF RDHLDYRFSH YRKIREAINQ YEGGLEVFSR GYEKLGFTRS VTGITYREWA
PGATWATLIG DFNNWNPNAD VMTRNEFGVW EIFLPNNADG SPAIPHGSRV KIRMDTPSGI
KDSIPAWINF SVQAPGAIPY DGIYYDPPEE ERYKFQHPRP KRPKSLRIYE CHIGMSSPEP
KINTYAEFRD DVLPRIKKLG YNALQIMAIQ EHSYYASFGY HVTNFFAPSS RFGTPDDLKS
LIDRAHELGL VVLMDIVHSH ASNNTLDGLN MFDGTDSCYF HSGTRGYHWM WDSRLFNYGN
WEVLRYLLSN ARWWLDEYKF DGFRFDGVTS MMYTHHGLSV GFTGNYSEYF GYATDVDAVV
YLMLVNDLIH GLFPEAITIG EDVSGMPTFC IPVRDGGVGF DYRLHMAIPD KWIEILKRRD
EDWQMGEIVH TLTNRRWLEK CVSYAESHDQ ALVGDKTIAF WLMDKDMYDF MALDRPATPV
IDRGIALHKM IRLITMGLGG EGYLNFMGNE FGHPEWIDFP RGEQRLPDGS VLPGNNFSYD
KCRRRFDLGD ADYLRYRGMQ EFDQAMHHLE EKYGFMTAKH QYISRQDEGD RVIIFERGDL
VFVFNFHWTN SYSDYRVGCL KPGKYKVALD SDSPLFGGFG RVQPDAEFFT FEGYHDDRPR
SFMVYAPSRT AVVYALAKEE DEAKPVEE
//
