ID   GLGB2_PEA               Reviewed;         826 AA.
AC   Q41059;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=1,4-alpha-glucan-branching enzyme 1, chloroplastic/amyloplastic;
DE            EC=2.4.1.18;
DE   AltName: Full=Starch branching enzyme I;
DE   Flags: Precursor; Fragment;
GN   Name=SBEII;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 58-72, FUNCTION,
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=7894509; DOI=10.1046/j.1365-313x.1995.07010003.x;
RA   Burton R.A., Bewley J.D., Smith A.M., Bhattacharyya M.K., Tatge H.,
RA   Ring S., Bull V., Hamilton W.D., Martin C.;
RT   "Starch branching enzymes belonging to distinct enzyme families are
RT   differentially expressed during pea embryo development.";
RL   Plant J. 7:3-15(1995).
CC   -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages
CC       in starch by scission of a 1,4-alpha-linked oligosaccharide from
CC       growing alpha-1,4-glucan chains and the subsequent attachment of the
CC       oligosaccharide to the alpha-1,6 position. May preferentially transfer
CC       long chains during branching. {ECO:0000269|PubMed:7894509}.
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   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stipules, pods and
CC       flowers. {ECO:0000269|PubMed:7894509}.
CC   -!- DEVELOPMENTAL STAGE: Very lov expression in young embryos, increasing
CC       during maturation. {ECO:0000269|PubMed:7894509}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X80010; CAA56320.1; -; mRNA.
DR   PIR; T06494; T06494.
DR   AlphaFoldDB; Q41059; -.
DR   SMR; Q41059; -.
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:0009507; C:chloroplast; 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: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   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   1: Evidence at protein level;
KW   Amyloplast; Chloroplast; Direct protein sequencing; Plastid; Transferase;
KW   Transit peptide.
FT   TRANSIT         <1..58
FT                   /note="Chloroplast"
FT   CHAIN           59..826
FT                   /note="1,4-alpha-glucan-branching enzyme 1,
FT                   chloroplastic/amyloplastic"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000146302"
FT   REGION          782..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..813
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        409
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        464
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   826 AA;  94191 MW;  46B9D1965CB5EC9C CRC64;
     ATTTTTTHNS KNKQYLAKQK PVELTLGYQN PNGCKVCSFG SKGSIYQKVS SGFKGVSVMT
     DDKSTMPSVE EDFENIGILN VDSSLEPFKD HFKYRLKRYL HQKKLIEEYE GGLQEFAKGY
     LKFGFNREED GISYREWAPA AQEAQIIGDF NGWNGSNLHM EKDQFGVWSI QIPDADGNPA
     IPHNSRVKFR FKHSDGVWVD RIPAWIKYAT VDPTRFAAPY DGVYWDPPLS ERYQFKHPRP
     PKPKAPRIYE AHVGMSSSEP RINSYREFAD DVLPRIRENN YNTVQLMAVM EHSYYASFWY
     HVTKPFFAVS SRSGSPEDLK YLIDKAHSLG LNVLMDVIHS HASNNVTDGL NGFDVGQSSQ
     QSYFHAGDRG YHKLWDSRLF NYANWKSSFL LSNLRWWLEE YKFDGFRFDG VTSMLYHHHG
     INMAFTGDYN EYFSEETDVD AVVYLMLANS LVHDILPDAT DIAEDVSGMP GLGRPVSEVG
     IGFDYRLAMA IPDKWIDYLK NKKDSEWSMK EISLNLTNRR YTEKCVSYAE SHDQSIVGDK
     TIAFLLMDEE MYSSMSCLTM LSPTIERGIS LHKMIHFITL ALGGEGYLNF MGNEFGHPEW
     IDFPREGNGW SYEKCRLTQW NLVDTNHLRY KFMNAFDRAM NLLDDKFSIL ASTKQIVSST
     NNEDKVIVFE RGDLVFVFNF HPENTYEGYK VGCDLPGKYR VALDSDATEF GGHGRVGHDA
     DQFTSPEGIP GIPETNFNNR PNSFKVLSPP HTCVVYYRVD ERQEESNNPN LGSVEETFAA
     ADTDVARIPD VSMESEDSNL DRIEDNSEDA VDAGILKVER EVVGDN
//