GLGB2_PEA
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 25-MAY-2022, entry version 95.
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).
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 PRIDE; Q41059; -.
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 Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 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; PTHR43651; 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; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 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
